WD-40 derived peptides and uses thereof

ABSTRACT

The present invention relates to a polypeptide composition effective to alter the activity of a first protein that interacts with a second protein, where the second protein contains at least one WD-40 region. The polypeptides of the present invention typically have between 4 and 50 amino acids whose sequence is the same as a sequence of the same length in the WD-40 region of the second protein. The invention further includes a method of altering the activity of the above described first protein. In one embodiment of the invention the polypeptide composition is effective to alter the activity of a protein kinase C, where the protein kinase C interacts with a second protein, and the second protein contains at least one WD-40 region (e.g., RACK1).

This application is a continuation-in-part of the parent applicationSer. No. 08/190,802 filed on Feb. 1, 1994 now U.S. Pat. No. 5,519,003.

FIELD OF THE INVENTION

the present invention relates in general to composition and methods ofmodulating the function of proteins involved in protein-proteininteractions. It relates more specifically to modulating the function ofa first protein of a pair of interacting proteins wherein a secondprotein of the pair contains a “WD-40” or “β-transducin” amino acidrepeat motif.

BACKGROUND ART

Many intracellular processes are carried out or regulated bymulti-subunit protein complexes that become active or repressed by theassociation or dissociation of individual polypeptide subunits.

One such group or family of proteins is related to the subunit oftransducin. Members of this group are all at least somewhat homologousto the β-subunit of transducin at the amino acid level, and contain avarying number of repeats of a particular motif identified inβ-transducin. The repeats have been termed “β-transducin”, or “WD-40”repeats (Fong, et al.).

Among the members of this protein family (Duronio, et al.) are the Gβsubunits that couple many receptors to their intracellular effectormolecules, Gβ/γ subunits that anchor another protein kinase (theβ-adrenergic receptor kinase, βARK), DNA binding proteins and yeast cellcycle proteins. All of these require a transient protein-proteininteraction for their function. However, the sequences at the interfaceof these proteins and their partners have not been identified.

The following are the references cited above and throughout thespecification:

U.S. PATENT DOCUMENTS

Crea, R., U.S. Pat. No. 4,888,286, issued Dec. 19, 1989.

Eaton, M. A. W., et al., U.S. Pat. No. 4,719,180, issued Jan. 12, 1988.

Yoshio, T., et al., U.S. Pat. No. 4,849,350, issued Jul. 18, 1989.

OTHER REFERENCES

Ausubel, F. M., et al., Current Protocols in Molecular Biology, JohnWiley and Sons, Inc., Media Pa.

Bohinski, R. C., Modern Concepts in Biochemistry, Second Edition, Allynand Bacon, Inc.

Dayhoff, M. O., in Atlas of Protein Sequence and Structure (1972) Vol.5, National Biomedical Research Foundation, pp. 101-110, and Supplement2 to this volume, pp. 1-10.

Duronio, R. J., et al., (1992) Proteins: Structure, Function, andGenetics 13:41-56.

Escobedo, J. A., et al., Mol. Cell. Biol., 11:1125-1132 (1991).

Fong, et al., (1986) Proc Natl Acad Sci USA 83:2162-2166.

Hari, et al., Endocrinology, 120:829-831 (1987).

Kleuss, C., et al., Science 259:832-834 (1993).

Makowske, O. M. and Rosen, O. M. J. Biol. Chem. 264:16155-16159 (1989)

Maniatis, T., et al., Molecular Cloning: A Laboratory Manual, ColdSpring Harbor Laboratory (1982).

Miller, J. F., et al., Nature (London) 216:659-63 (1969).

Mochly-Rosen, D., and Koshland, D. E., Jr. J. Biol. Chem. 262:2291-2297(1987).

Mochly-Rosen, et al., Molec. Biol. Cell. 1:693-706 (1990).

Mochly-Rosen, D., et al., Proc. Natl. Acad. Sci. USA 88:3997-4000(1991).

Orr, J. W., et al., J. Biol. Chem. 267, 16155-16159 (1992)

Pitcher, J., et al., Science 257:1264-1267 (1992).

Reiner, et al., Nature 364:717-721 (1993).

Schulz, G. E. and R. H. Schirmer., Principles of Protein Structure,Springer-Verlag.

Smith, B. L. and Mochly-Rosen, D. Biochem. Biophys. Res. Commun.188:1235-1240 (1992).

Smith, D. B., et al., Gene 67:31 (1988).

Stith, B. J. and J. L. Maller. Exp. Cell. Res. 169:514-523 (1987).

Wolf, M. and N. Sahyoun, Chem., 261:13327-13332 (1986).

DISCLOSURE OF THE INVENTION

The invention includes, in one aspect, a polypeptide compositioneffective to alter the activity of a first protein, such as proteinkinase C, or β-adrenergic receptor kinase (βARK). The polypeptide blocksor inhibits an interaction, such as a binding interaction, between thefirst protein and a second protein containing a WD-40 region.

The polypeptide contains between 4 and 50 amino acids whose sequence isthe same as a sequence of the same length in the WD-40 region of thesecond protein.

The polypeptide may block the binding of the first to the secondprotein, or may be an agonist or antagonist of the first protein. TheWD-40 region preferably has an amino acid sequence homologous oridentical to the sequences defined by SEQ ID NO:76-261.

In a second embodiment, the invention includes a method of altering theactivity of the first protein of the type defined above. The methodincludes selecting a polypeptide having between 4 and 50 amino acidswhose sequence is the same as a sequence of the same length in the WD-40region of the second protein, and contacting the polypeptide with thefirst protein under conditions which allow the formation of a complexbetween the polypeptide and the first protein, where this interactionalters the activity of the first protein.

In one embodiment, the contacting is effective to inhibit theinteraction between the first and second proteins. In anotherembodiment, the contacting is effective to stimulate the activity of thefirst protein.

In still another embodiment, the contacting is effective to inhibit theactivity of the first protein.

The polypeptide preferably has an amino acid sequence homologous oridentical to the sequences defined by SEQ ID NO:76-261.

In a more specific aspect of the invention, the invention includes apolypeptide composition effective to alter the activity of proteinkinase C, where the protein kinase C interacts with a second protein,and the second protein contains at least one WD-40 region. Thepolypeptide has between 4 and 50 amino acids whose sequence is the sameas a sequence of the same length in the WD-40 region of the secondprotein.

In a preferred embodiment, the second protein is a receptor foractivated protein kinase C, and has the sequence represented by SEQ IDNO:27.

In other specific embodiments, the polypeptide is (i) an agonist ofprotein kinase C, and the polypeptide has the sequence represented bySEQ ID NO:7; (ii) an antagonist of the activity of protein kinase C;and/or (iii) an inhibitor of the interaction between protein kinase Cand the second protein. In the latter embodiment, the polypeptide hassequence corresponding to SEQ ID NO:4 or SEQ ID NO:7.

The WD-40 region preferably has an amino acid sequence homologous oridentical to SEQ ID NO:69-75.

In a related embodiment, the invention includes a method of altering theactivity of a protein kinase C that interacts with a second protein,where said second protein contains at least one WD-40 region.

The method includes selecting a polypeptide having between 4 and 50amino acids whose sequence is the same as a sequence of the same lengthin the WD-40 region of the second protein, and contacting thepolypeptide with the protein kinase C under conditions which allow theformation of a complex between the polypeptide and the protein kinase C,where said interaction alters the activity of said protein kinase C.

Other aspects of the invention include the polypeptide compositions ofthe invention wherein said polypeptide is coupled to a solid support, aswell as a method to bind selectively said first protein which methodcomprises contacting a sample putatively containing said first proteinwith the polypeptide composition bound to solid support and removing anyunbound components of the sample from said composition.

In still another aspect, the invention relates to a method to assess theinteraction of a first protein with a polypeptide represented by anamino acid sequence contained in a second protein, wherein said secondprotein contains at least one WD-40 region, which method comprisescontacting a sample containing said first protein with a polypeptidecomposition wherein the polypeptide has between 4 and 50 amino acidswhose sequence is the same as the sequence of the same length in theWD-40 region of the second protein, and observing any interaction of thefirst protein with said polypeptide composition. The invention alsoconcerns a method to assess the ability of a candidate compound to binda first protein which method comprises contacting said first proteinwith a polypeptide composition which binds said first protein, whereinthe polypeptide of said composition has between 4 and 50 amino acidswhose sequence is the same as a sequence of the same length in a WD-40region of a second protein which interacts with said first protein, inthe presence and absence of said candidate compound; and measuring thebinding of said polypeptide in the presence and in the absence of saidcandidate, wherein decreased binding of the polypeptide in the presenceas opposed to the absence of said candidate indicates that saidcandidate binds to said first protein.

In still another aspect, the invention is directed to recombinantmaterials for the production of the polypeptides of the invention andmethods for their production.

These and other objects and features of the invention will become morefully apparent when the following detailed description of the inventionis read in conjunction with the accompanying drawings.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1A shows the cDNA sequence of rat brain RACK1.

FIG. 1B shows an amino acid self-homology matrix analysis of RACK1.

FIG. 1C shows the amino acid sequence of RACK1, aligned to show theseven WD-40 repeats represented in the molecule.

FIG. 2 shows the results of an overlay assay to detect PKC binding toimmobilized RACK1 in the presence and absence of PKC activators.

FIG. 3 shows the results of an overlay assay to detect PKC binding toimmobilized RACK1 in the presence and absence of WD-40-derived peptides.

FIG. 4 shows the results of an overlay assay to detect binding of βPKCto either peptide I (SEQ ID NO:1) or peptide rVI (SEQ ID NO:7)immobilized on nitrocellulose membranes under various conditions.

FIG. 5A shows the effects of injecting peptides I (SEQ ID NO:1) and rVI(SEQ ID NO:7) on PKC-mediated germinal vesicle breakdown (GVBD), ameasure of insulin-induced oocyte maturation.

FIG. 5B shows the effects of injecting peptides I (SEQ ID NO:1) and rVI(SEQ ID NO:7) on PKC-mediated germinal vesicle breakdown (GVBD) in theabsence of insulin induction.

FIG. 5C shows the effects of injecting peptide rIII (SEQ ID NO:4) onPKC-mediated germinal vesicle breakdown (GVBD) in the absence of insulininduction.

FIG. 6 shows the distribution of βPKC in Xenopus oocytes between thecytosolic and membrane-associated fractions following microinjection ofeither injection solution, peptide I (SEQ ID NO:1) or peptide rVI (SEQID NO:7) with or without insulin stimulation.

FIG. 7 shows the effects of peptides I and rVI on the sensitivity ofβPKC to Arg-C endopeptidase.

FIG. 8 shows the effects of peptides I and rVI on PKCautophosphorylation in the absence of PKC activators.

FIG. 9 shows the effects of peptides I and rVI on PKC phosphorylation ofhistones in the absence of PKC activators.

FIG. 10 shows the effects of peptide rIII on PKC phosphorylation ofhistones in the absence of PKC activators.

FIG. 11 shows the amino acid sequence of the 56 kDa human protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 12 shows the amino acid sequence of the AAC-rich protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 13 shows the amino acid sequence of the B-TRCP protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 14 shows the amino acid sequence of the Beta-prime-COP protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 15 shows the amino acid sequence of the CDC4 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 16 shows the amino acid sequence of the Chlam-3 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 17 shows the amino acid sequence of the COP-1 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 18 shows the amino acid sequence of the CORO protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 19 shows the amino acid sequence of the Coronin p55 protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 20 shows the amino acid sequence of the Cstf 50 kDa protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 21 shows the amino acid sequence of the bovine G-beta-1 proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 22 shows the amino acid sequence of the bovine G-beta-2 proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 23 shows the amino acid sequence of the drosophila G-beta proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 24 shows the amino acid sequence of the human G-beta-1 protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 25 shows the amino acid sequence of the human G-beta-2 protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 26 shows the amino acid sequence of the mouse G-beta protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 27 shows the amino acid sequence of the drosophila groucho proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 28 shows the amino acid sequence of the squid GTP-binding proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 29 shows the amino acid sequence of the HSIEF 930 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 30 shows the amino acid sequence of the human 12.3 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 31 shows the amino acid sequence of the human IEF-7442 protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 32 shows the amino acid sequence of the insulin-like growth factorbinding protein complex with the WD-40 repeats aligned and putativebinding peptide regions delineated by a box.

FIG. 33 shows the amino acid sequence of the rat insulin-like growthfactor binding protein with the WD-40 repeats aligned and putativebinding peptide regions delineated by a box.

FIG. 34 shows the amino acid sequence of the human LIS1 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 35 shows the amino acid sequence of the MD6 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 36 shows the amino acid sequence of the yeast MSI1 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 37 shows the amino acid sequence of the mouse pc326 MUS proteinwith the WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 38 shows the amino acid sequence of the ORD RB1 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 39 shows the amino acid sequence of the periodic trp protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 40 shows the amino acid sequence of the PLAP protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 41 shows the amino acid sequence of the retinoblastoma bindingprotein with the WD-40 repeats aligned and putative binding peptideregions delineated by a box.

FIG. 42 shows the amino acid sequence of the S253 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 43 shows the amino acid sequence of the SOF1 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 44 shows the amino acid sequence of the STE4 yeast protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 45 shows the amino acid sequence of the TF1 transcription factorprotein with the WD-40 repeats aligned and putative binding peptideregions delineated by a box.

FIG. 46 shows the amino acid sequence of the TUP1 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 47 shows the amino acid sequence of the TUP1 homolog protein withthe WD-40 repeats aligned and putative binding peptide regionsdelineated by a box.

FIG. 48 shows the amino acid sequence of the YCU7 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 49 shows the amino acid sequence of the YCW2 protein with the WD-40repeats aligned and putative binding peptide regions delineated by abox.

FIG. 50 shows the amino acid sequence of the YKL25 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

FIG. 51 shows the amino acid sequence of the YRB140 protein with theWD-40 repeats aligned and putative binding peptide regions delineated bya box.

DETAILED DESCRIPTION OF THE INVENTION

I. Definitions

Unless otherwise indicated, all terms used herein have the same meaningas they would to one skilled in the art of the present invention.Practitioners are particularly directed to Current Protocols inMolecular Biology (Ausubel) for definitions and terms of the art.

Abbreviations for amino acid residues are the standard 3-letter and/or1-letter codes used in the art to refer to one of the 20 common L-aminoacids. Likewise, abbreviations for nucleic acids are the standard codesused in the art.

An “amino acid group” refers to a group of amino acids where the groupis based on common properties, such as hydrophobicity, charge, or size.

A “conserved set” of amino acids refers to a contiguous sequence ofamino acids that is conserved between members of a group of proteins. Aconserved set may be anywhere from two to over 50 amino acid residues inlength. Typically, a conserved set is between two and ten contiguousresidues in length. The individual positions within a conserved set eachtypically comprise one of several amino acids, selected from an aminoacid group(s). In cases where a residue is 100% conserved at aparticular position, the conserved set sequence will contain only thatresidue at that position. For example, for the two peptides WRTAA (SEQID NO:263) and WRTAV (SEQ ID NO:264), there are 4 identical positions(WRTA; SEQ ID NO:265) and one position where the residue is an “A” or a“V”.

Proteins are typically long chains of amino acid based polyamides(polypeptides) capable of creating secondary and tertiary structure.Proteins may be composed of one, two or more polypeptide chains and mayfurther contain some other type of substance in association with thepolypeptide chain(s), such as metal ions or carbohydrates. The size ofproteins covers a rather wide range from ˜5,000 to several hundredthousand g/mole. The 5,000 figure corresponds to the presence or roughly40-45 amino acids.

Unless otherwise indicated, the sequence for proteins and peptides isgiven in the order from the amino terminus to the carboxyl terminus.Similarly, the sequence for nucleic acids is given in the order from the5′ end to the 3′ end.

The term “interacting proteins” refers to a pair of polypeptides thatcan form a stably-associated complex due to, for example, electrostatic,hydrophobic, ionic and/or hydrogen-bond interactions under physiologicalconditions.

Proteins smaller than about 5,000 g/mole are typically referred to aspolypeptides or simply peptides (Bohinski).

Two amino acid sequences or two nucleotide sequences are consideredhomologous (as this term is preferably used in this specification) ifthey have an alignment score of >5 (in standard deviation units) usingthe program ALIGN with the mutation gap matrix and a gap penalty of 6 orgreater (Dayhoff). The two sequences (or parts thereof) are morepreferably homologous if their amino acids are greater than or equal to50%, more preferably 70%, still more preferably 80%, identical whenoptimally aligned using the ALIGN program mentioned above.

A peptide or peptide fragment is “derived from” a parent peptide orpolypeptide if it has an amino acid sequence that is identical orhomologous to the amino acid sequence of the parent peptide orpolypeptide. Homologous peptides are defined above. Exemplary derivedpeptides are peptide rIII (SEQ ID NO:4) and peptide rVI (SEQ ID NO:7),which are derived from the third and seventh WD-40 repeats of RACK1 (SEQID NO:27), respectively.

The term “expression vector” refers to vectors that have the ability toincorporate and express heterologous DNA fragments in a foreign cell.Many prokaryotic and eukaryotic expression vectors are commerciallyavailable. Selection of appropriate expression vectors is within theknowledge of those having skill in the art.

The term “PKC” refers to protein kinase C, or C-kinase.

The term “RACK” refers to receptor for activated C-kinase.

The term “PS” refers to phosphatidylserine.

The term “DG” refers to diacylglycerol.

The term “PL” refers to phospholipids. Phospholipids include bothphosphatidylserine and diacylglycerol.

The term “GVBD” refers to germinal vesicle breakdown, a measure ofinsulin-induced maturation in Xenopus oocytes.

The term “PCR” refers to polymerase chain reaction.

The term “NMR” refers to nuclear magnetic resonance.

The term “βARK” refers to β-adrenergic receptor kinase.

II. General Overview of Invention

The invention relates to interacting proteins, at least one of whichcontains an amino acid sequence with one or more of the characteristicrepeats termed WD-40 (Fong, et al.).

According to one aspect of the invention, the function of a firstprotein of a pair of interacting proteins may be modulated, altered ordisrupted by the addition, to a solution or medium containing theprotein, of a peptide having a sequence that is identical or homologousto a part of the sequence of a WD-40 motif-containing repeat present ina second protein of the pair of interacting proteins.

The modulation or disruption of function of the first protein is due tothe binding or association of the WD-40-derived peptide, termed “bindingpeptide”, with the first protein. The consequences of the binding orassociation of the binding peptide with the first protein depend on thesequence of the peptide.

Typically, the presence of the binding peptide will inhibit the bindingof the first protein to the second protein. This binding may be assayedin vitro by, for example, an overlay assay, whereby the degree ofbinding of one protein to another may be assessed. Several adaptationsof overlay assays applied to embodiments of the present invention aredescribed herein.

Regardless of whether or not the WD-40-derived peptide affects theassociation of the first protein with the second protein, the peptidemay alter or modulate defined activities of the first protein. Theseactivities may be assayed by a variety of methods in vivo and/or invitro. The method(s) employed depend on the protein whose activity isbeing measured.

An exemplary first protein of a pair of interacting proteins is proteinkinase C (PKC). Upon activation, PKC interacts with receptors foractivated C kinase (RACKs), at least one of which (RACK1) contains WD-40repeats. Several assays for determining the activity of PKC in thepresence and in the absence of peptides derived from the WD-40 region ofRACK1 are detailed herein.

Certain “interacting proteins” interact only after one or more of themhas been stimulated by an exogenous or endogenous factor(s). Forinstance, PKC, as shown herein, does not bind to RACK proteins until ithas been activated by, for example, phosphatydilserine (PS),diacylglycerol (DG) and calcium. However, peptides derived from WD-40repeats of a second protein of such a pair may be able to associate withor bind to the first protein even in the absence of activators of thefirst protein, and in so doing, affect the function of the first protein(e.g. activate, inactivate, potentiate, sensitize, desensitize, alterthe specificity, etc.).

Binding peptides derived from WD-40 repeats of a second protein of apair of interacting proteins, may be useful as specific agonists,antagonists, potentiators of function, and the like, of the firstprotein of the pair. These properties may make the peptides useful in anumber of applications, for example, direct use in therapeuticapplications or as lead compounds for the development of othertherapeutic agents, e.g., small organic molecules.

III. Advantages of the Invention for the Inhibition of Activated PKCBinding to RACK1

Protein kinase C (PKC) is a family of at least 10 isozymes that sharecommon structures and biochemical characteristics. It has beendemonstrated that several isozymes are present within a single celltype, and it has been assumed that individual PKC isozymes are involvedin different cellular functions. However, so far, the availableactivators and inhibitors of PKC do not appear to be isozyme-specific.Therefore, it is currently impossible to determine the role ofindividual PKC isozymes in normal cellular functions as well as indisease.

PKC activation by, for example, diacylglycerol and calcium, induces thetranslocation of PKC from a soluble (cytosolic) to a cell particulate(membrane-associated) fraction, as shown in experiments herein (Example8). Activated PKC is stabilized in the cell particulate fraction bybinding to membrane-associated receptors (receptors for activatedC-Kinase, or RACKs).

In experiments done in support of the present invention and describedherein, a clone (pRACK1) encoding a RACK has been isolated (Example 1).RACK1 belongs to a growing family of proteins that are homologous to theβ-subunit of transducin and contain the WD-40 motif (Fong, et al.). Itwas demonstrated that peptide I (SEQ ID NO:1) binds to purified PKC (seeExample 6 and FIG. 4), inhibits the binding of PKC to purifiedrecombinant RACK1 protein (see Example 4 and FIG. 3), and inhibits PKCactivity in several in vivo and in vitro assays (see Examples 7-11 andFIGS. 5-9).

Peptide I (SEQ ID NO:1) is homologous to a sequence identified in thesixth WD-40 repeats of RACK1 (see FIG. 1C). A synthetic peptide wasprepared based on this sequence (peptide rVI; SEQ ID NO:7; underlinedamino acids in repeat VI of FIG. 1C). Six more peptides were alsoprepared based on the corresponding regions in repeats I-V and VII(peptides rI-rV, rVII; SEQ ID NO:2-6, 8; underlined regions incorresponding repeats, FIG. 1C). Some of the peptides were also found toinhibit the binding of PKC to RACK1 (see Example 4 and FIG. 3). Inaddition, some of the peptides were found to bind to purified PKC (seeExample 6, FIG. 4), partially activate PKC in the absence of otheractivators (peptide rVI; see Examples 7, 10, 11 and FIGS. 5, 8 and 9,and potentiate the effects of known PKC activators on the enzyme (seeExamples 7-9 and FIGS. 5-7).

In Xenopus oocyte maturation studies (see, for instance, Example 7),peptide rVI (SEQ ID NO:7) is an agonist of βPKC. Peptide rIII, whileless potent, is also an agonist of PKC; it enhances insulin-inducedoocyte maturation at 50 and 500 μM.

In cardiac myocytes, norepinephrine (NE, 2 μM) causes translocation of δand εPKC isozymes from the cytosolic to the particulate fraction.Introduction into cardiac myocytes of peptide rIII, and to a lesserextent peptide rVI, caused an immediate translocation of δ and εPKCisozymes in the absence of hormone stimulation. This peptide-inducedtranslocation was followed by degradation of δ and εPKC isozymes.Moreover, NE-induced translocation is further enhanced in cellscontaining peptide rIII.

In contrast, introduction of peptide I to these cells does not affectPKC distribution in the absence of hormone stimulation, nor does itinduce PKC degradation. Furthermore, NE-induced translocation isinhibited by peptide I. Similar concentrations of a number of controlpeptides did not affect PKC distribution or degradation in control orNE-treated cells.

In studies on rat cardiac myocytes, peptide rIII induced δPKC and εPKCactivation that was followed by degradation of these activated isozymes.

Peptide rVI also augments hormone-induced translocation of PKC isozymes(see, for example, Example 8 and FIG. 6). In contrast, peptide I (SEQ IDNO:1) inhibited hormone-induced translocation of PKC isozymes (Example8, FIG. 6) and did not cause degradation.

The data summarized above demonstrate that peptides derived from WD-40repeats of RACK1 can serve as PKC agonists and antagonists in vivo, andsuggest that peptides derived from WD-40 regions of RACK1 contain atleast part of the protein-protein interface between PKC and RACK1.

Furthermore, the results suggest that (i) WD-40 repeats present in otherproteins, such as Gβ subunit, may also be located at or near a surfaceinvolved in protein-protein interactions, (ii) peptides derived fromthese repeats may be effective in disrupting the interactions of theproteins with their partners (e.g. β-adrenergic receptor kinase (βARK),(iii) the peptides may modulate or alter the activity of the proteinswith which the WD-40 repeat-containing proteins interact, and (iv) thepeptides may therefore have specific biological effects whenadministered in vivo.

IV. Identification of Pairs of Interacting Proteins

A. Biochemical Approaches

Novel interacting proteins may be identified and isolated by a number ofmethods known to those skilled in the art. For example, monoclonalantibodies raised to a mixture of antigens, such as a particular tissuehomogenate, may be characterized and used to immunoprecipitate a singleclass of antigen molecules present in that tissue. The precipitatedproteins may then be characterized further, and used to co-precipitateother proteins with which they normally interact (Hari, et al.,Escobedo, et al.).

An alternate method to identify unknown polypeptides that interact witha known, isolated protein is by the use of, for example, an overlayassay (Wolf, et al., Mochly-Rosen, et al., 1991). A mixture (such as afraction of a tissue homogenate, for example, a Triton-insoluble proteinfraction) potentially containing proteins that bind to a known, isolatedprotein can be resolved using PAGE, blotted onto a nitrocellulose ornylon membrane, and contacted with a solution containing the knownprotein and any necessary co-factors or small molecules. After washing,the membrane can be contacted with a probe for the known protein, forexample an antibody or a mixture of antibodies, and the signalvisualized.

B. Molecular Approaches

Putative binding proteins of a known protein may be isolated from tissuehomogenates, as described above. Alternatively, DNA clones encodingputative binding proteins may be identified by screening, for example,an appropriate cDNA expression library. Expression libraries made from awide variety of tissues are commercially available (for example, fromClonetech, Palo Alto, Calif.). Expression libraries may also be made denovo from organisms and tissues of choice by practitioners skilled inthe art.

The screening of expression libraries for clones expressing a protein orprotein fragment of interest may be readily accomplished usingtechniques known in the art, for example, an overlay assay.

An overlay-assay screening method may be used to identify clonesexpressing a (known or unknown) protein or protein fragment that bindsto a probe in hand. The probe may be a protein postulated to be involvedin protein-protein interactions with a protein expected to be present ina cDNA library selected for screening (as was the case for the cloningof RACK1, detailed in Example 1).

Actual screening of a selected cDNA library may be accomplished byinducing plated clones to express cloned exogenous sequences,transferring replicas of the induced plaques or colonies to filtermembranes, and screening the membranes with an appropriate probe.According to this method, lifts of filters (for example, nylon ornitrocellulose) from an appropriately-induced cDNA library plates(induced by, for example, IPTG) are washed, blocked, and incubated witha selected probe for a period of time sufficient to allow the selectedprobe(s) to bind specifically to polypeptide fragments present on thefilters. The filters may then be washed and reacted with a reagent (forexample, antibodies such as alkaline phosphatase-conjugated goatanti-rabbit or anti-mouse antibodies, available from Boehringer MannheimBiochemicals, Indianapolis, Ind.). Additional reactions may be carriedout as required to detect the presence of bound probe.

One such overlay assay, described in Example 1, was used to screen a ratbrain cDNA expression library for proteins that bind purified PKC in thepresence of PKC activators (phosphatydilserine, diacylglycerol andcalcium). The filters were screened with a mixture of rat brain PKCisozymes (α, β, γ, δ, ε and ζ). Following a series of washes, bound PKCisozymes were detected with a mixture of anti-α, β, γ PKC mousemonoclonal antibodies, and anti-δ, ε and ζ PKC rabbit polyclonalantibodies. Bound antibodies were detected using alkalinephosphatase-conjugated goat anti-rabbit or anti-mouse antibodies and5-bromo-4-chloro-3-indoyl phosphate p-toluidine salt as a substrate.

Once a clone is identified in a screen such as the one described above,it can be isolated or plaque purified and sequenced. The insert may thenbe used in other cloning reactions, for example, cloning into anexpression vector that enables efficient production of recombinantfusion protein. Examples of appropriate expression vectors are pGEX(Smith, et al., 1988) and pMAL-c2 (New England BioLabs, Beverly, Mass.).An expression vector containing an insert of interest may be used totransform appropriate host cells, such as E. coli, and the transformedhost cells can be used to produce the recombinant protein in largeamounts.

Typically, a recombinant protein is expressed in tandem with a bacterialor viral gene product (endogenous polypeptide) as part of a fusionprotein. The junction between the endogenous polypeptide and therecombinant protein typically includes a recognition site for arare-cutting protease. The endogenous peptide may be designed toincorporate a unique affinity tag (a short peptide sequence) tofacilitate the purification of the fusion protein with an affinityreagent, such an antibody directed against the affinity tag. Therecombinant protein may then be purified from the fusion protein usingthe appropriate protease.

Purified recombinant protein may be used in a number of ways, includingin an overlay binding assay to screen for peptides or substances thatinhibit binding between the recombinant protein and an interactingprotein.

An example of the use of a cDNA clone to express protein is detailed inExample 2. RACK1 cDNA, isolated as described above and in Example 1, wassubcloned into an expression vector (pMAL-c2, New England BioLabs,Beverly, Mass.) capable of expressing a cloned insert in tandem withmaltose-binding protein (MBP). The vector containing the RACK1 insertwas used to transform TB1 E. coli, which were then induced with IPTG.The cells produced a 78 kDa fusion protein comprised of RACK1 fused tothe MBP. The overexpressed fusion protein was purified on an amyloseaffinity column according to the manufacture's protocol (New EnglandBioLabs, Beverly, Mass.) and incubated with protease Xa to separate theexpressed insert from the MBP. Following the incubation, a 36 kDa RACK1protein was obtained.

V. Identification of WD-40 Repeats

According to a method of the present invention, protein-proteininteractions can be disrupted and/or the activity of an interactingprotein can be altered, given at least one of the interacting proteinscontains a WD-40 motif, or region, with a peptide(s) derived from aWD-40 repeat(s) of one of the proteins.

WD-40 repeats are typically found in a family of proteins having atleast a limited homology with the β subunit of transducin. WD-40 repeatspresent in a selected member of this family can be identified by (A)performing a self-homology analysis on a selected protein using ahomology matrix (performed by, for example, the computer program DNAStrider 1.2, available from Christian Marck, Service de Biochemie et deGenetique Moleculaire, Department de Biologie Cellulaire et Moleculaire,Direction des Sciences de la Vie-CEA-FRANCE), (B) aligning sequencescomprising the repeating elements revealed by the homology matrixanalysis, and (C) identifying conserved amino acid residues thattypically serve to define a WD-40 repeat. The steps are discussedindividually, below.

A. Homology Matrix Analysis

Determining whether a particular amino acid sequence contains repeatedmotifs may be accomplished by a number of methods known to those skilledin the art. They range from a simple visual inspection of the sequenceto the use of computer programs which can identify repeated motifs. Onewidely-implemented computer-assisted method is to generate aself-homology matrix. A self-homology matrix computes the homology ofeach amino acid residue in a particular sequence with every otherresidue in that sequence. The homology scores are stored in a2-dimensional matrix.

Values higher than a selected criterion level are flagged and displayedas points on an x-y coordinate. The x- and y-axes correspond toconsecutive amino acid positions in the sequence.

An example of a self-homology matrix analysis is shown in FIG. 1B. Thematrix was generated using the computer program DNA Strider 1.2(Christian Marck, Service de Biochemie et de Genetique Moleculaire,Department de Biologie Cellulaire et Moleculaire, Direction des Sciencesde la Vie-CEA-FRANCE) with the amino acid sequence of RACK1 (SEQ IDNO:27) with a window setting of 21 and a stringency of 6. Some typicalfeatures of a self-homology matrix are evident in the figure. The graphshows a “primary” diagonal line extending from the origin with a slopeof unity, corresponding to the fact that the sequence is identical toitself. If the sequence contains repeating elements, as RACK1 does,there will be other, shorter sets of contiguous points arranged indiagonal lines substantially parallel to the primary diagonal and offsetfrom the primary diagonal in the x- or y-directions. These shorter linesidentify the locations of repeating elements with the sequence. Eachrepeating element will result in two sets of displayed points,symmetrically distributed about the primary diagonal.

The data displayed in a homology matrix analysis can be used to locateand roughly align the sequences of repeating elements for a moredetailed analysis. The horizontal band delineating the region between˜100 and ˜130 on the y-axis in FIG. 1B highlights the fact that portionsof that region of RACK1, that is, the amino acids between about aminoacid 100 and amino acid 130, are repeated a total of seven times in thesequence of RACK1. Arrows point to the repeats in the homology matrix.For purposes of rough alignment, the short diagonal lines pointed out bythe arrows can be extended to the horizontal line at amino acid ˜100 onthe y-axis, and the x-axis location corresponding to the intersection benoted. For example, the intersection corresponding to the second repeat(second arrow from the left) is at x=˜50).

Values determined in this manner may then be used to align the aminoacid sequence of the repeats with each consecutive repeat beneath thepreceding one, the start of each repeat corresponding approximately tothe amino acid position determined by the analysis in the precedingparagraph. The amino acid sequence of RACK1, aligned in this manner, isshown in FIG. 1C.

Most commercially-available DNA and protein sequence analysis programshave the capability to perform a self-homology matrix analysis. Oneexample is the program DNA Strider 1.2 (Christian Marck, Service deBiochemie et de Genetique Moleculaire, Department de Biologie Cellulaireet Moleculaire, Direction des Sciences de la Vie-CEA-FRANCE).

Once the repeating elements are identified and the sequencescorresponding to repeating elements are roughly aligned, one may proceedto define the degree of homology among the individual repeats at thespecific positions within the repeats, as is described below.

B. Aligning Amino Acid Sequences

If a self-homology matrix was used to obtain a crude alignment, thesequences may aligned by eye on a personal computer or the like using,for example, a text editor, a drawing program or a sequence-analysisprogram. Examples of programs effective to accomplish an alignmentinclude “MACDRAW PRO” (Claris Corp., Santa Clara, Calif.) and “WORD”(Microsoft Corp., Redmond, Wash.), both of which are available for“MACINTOSH” series computers (Apple Computer Corporation, Cupertino,Calif.), as well as IBM-compatible computers running “WINDOWS”(Microsoft Corp.).

Amino acid sequences corresponding to internal repeats can also bealigned automatically using a protein sequence analysis program, such as“MACVECTOR” (Eastman Kodak Co., New Haven, Conn.).

According to a method of the invention, aligned sequences are examinedfurther to determine if they fulfil criteria to be defined as WD-40repeats. These criteria are detailed in part C, below.

C. Amino Acid Residues that Define a WD-40 Repeat

Upon completion of steps outlined in parts A and B above, that is,determining whether a particular protein contains internal repeats, andif so, aligning those repeats, it is necessary to determine whether thealigned repeats contain WD-40 regions.

A WD-40 motif is roughly defined as a contiguous sequence of about 25 to50 amino acids with relatively-well conserved sets of amino acids at thetwo ends (amino- and carboxyl-terminal) of the sequence. Conserved setsof at least one WD-40 repeat of a WD-40 repeat-containing proteintypically contain conserved amino acids at certain positions. Theamino-terminal set, comprised of two contiguous amino acids, oftencontains a Gly followed by a His. The carboxyl-terminal set, comprisedof six to eight contiguous amino acids, typically contains an Asp at itsfirst position, and a Trp followed by an Asp at its last two positions.

A more accurate definition of a WD-40 motif incorporates the observationthat while specific residues, such as those identified above, are notalways conserved within a WD-40 motif, conserved positions within themotif are typically occupied by residues selected from a restrictedclass of amino acids.

In order to better define the class of conserved residues at selectedpositions, it is necessary to group amino acids on the basis of certaincommon properties. A functional way to define common properties betweenindividual amino acids is to analyze the normalized frequencies of aminoacid changes between corresponding proteins of homologous organisms(Schulz). According to such analyses, groups of amino acids may bedefined where amino acids within a group exchange preferentially witheach other, and therefore resemble each other most in their impact onthe overall protein structure (Schulz). Examples of amino acid groupsdefined in this manner, some of which are used in the definition of aWD-40 motif herein, include:

(i) a charged group, consisting of Glu and Asp, Lys, Arg and His,

(ii) a positively-charged group, consisting of Lys, Arg and His,

(iii) a negatively-charged group, consisting of Glu and Asp,

(iv) an aromatic group, consisting of Phe, Tyr and Trp,

(v) a nitrogen ring group, consisting of His and Trp,

(vi) a large aliphatic nonpolar group, consisting of Val, Leu and Ile,

(vii) a slightly-polar group, consisting of Met and Cys,

(viii) a small-residue group, consisting of Ser, Thr, Asp, Asn, Gly,Ala, Glu, Gln and Pro,

(ix) an aliphatic group consisting of Val, Leu, Ile, Met and Cys, and

(x) a small hydroxyl group consisting of Ser and Thr.

In addition to the groups presented above, each amino acid residue mayform its own group, and the group formed by an individual amino acid maybe referred to simply by the one and/or three letter abbreviation forthat amino acid commonly used in the art.

A “WD-40” motif is defined herein as a contiguous set of amino acidsbetween (inclusive) two sets of relatively well conserved residues,termed herein as an “amino-terminal set” and a “carboxyl-terminal set”.

The amino-terminal set contains two adjacent amino acids. The residue atthe first position is typically selected from groups ii, vi or viii,while the residue at the second position is typically selected fromgroups i, x or Ile. The first and second positions will often consist ofGly and His, respectively. The Gly and His residues are typicallypresent in at least one of the aligned repeats of a WD-40-containingprotein.

The carboxyl-terminal conserved set typically includes eight residues,but may contain as few as six residues. The most well-conserved residuein WD-40 motifs identified thus far is an Asp residue, comprising thefirst amino acid of the carboxyl-terminal conserved set. It is presentin virtually all WD-40 repeats illustrated herein. In those repeatswhere it is not present, the position is occupied by a residue fromgroups iii or Gly.

The last two amino acids in the carboxyl-terminal conserved set aretypically selected from groups iv or Ile, and groups i or viii,respectively. The most commonly used residue at the first of thesepositions is Trp. It is typically present in at least one of the WD-40repeats of any given protein. The second position is occupied lessconsistently by a single residue, but is often occupied by Asp. TheTrp-Asp (WD) combination is part of the namesake of WD-40 repeats.

The amino acids present in the internal portion of the carboxyl-terminalconserved set are less well-conserved than the terminal residues, andtheir total number may differ by up to two residues in different WD-40repeats. The third position in from the carboxyl-terminal end of thecarboxyl-terminal conserved set is typically selected from groups viiior ix, more typically ix. The fifth position in from thecarboxyl-terminal end of the carboxyl-terminal conserved set is alsotypically selected from groups viii or ix, more typically ix.

The length of a WD-40 repeat, including the amino-terminal andcarboxyl-terminal conserved sets is typically between about 25 and about50 residues, more typically between about 29 and 34 residues. Thedistribution arises primarily from differences in the number of residuespresent between the amino-terminal and carboxyl-terminal conserved sets.

The number of WD-40 repeats in a particular protein can range from twoto more than eight. The average number is about 5.

A determination of whether or not a set of aligned internal repeats areWD-40 repeats can be facilitated by an examination of all of the repeatsas a whole, rather than an examination of each repeat individually. Thisis in part because not all of the aligned repeats will necessarilycontain all of the conserved sequences that serve to identify WD-40repeats, although the conserved residues will typically appear in atleast one of the repeats.

For example, FIG. 1C shows the RACK1 amino acid sequence aligned toillustrate the internal repeats present in the sequence. All of therepeats are WD-40 repeats, even though the amino-terminal conserved setof repeat VI, for instance, contains an “LD” as opposed to the moreusual “GH”, and the carboxyl-terminal conserved set contains a “G” atits first position, as opposed to the highly-conserved “D”. Similarly,the carboxyl-conserved set of, for example, repeat I, contains a “WK” atthe last to positions, as opposed to the more usual “WD”.

It will be appreciated that certain residues or sets of residues will bewell-conserved in the WD-40 repeats of a selected protein, even thoughthey may not be conserved in WD-40 repeats in general. Such residues orsets of residues may be useful in several ways. For example, they may beused in performing an alignment of internal repeats in a selectedprotein, as described in part B, above. The residues may also be usefulfor identifying regions based on which effective binding peptides may bedesigned (see section VI., below).

D. Identification of WD-40 Repeats in RACK1

In experiments done in support of the present invention, a protein thatbinds to activated PKC was cloned and sequenced (see Example 1).Sequence analysis of the deduced amino acid sequence revealed thepresence of repeats, which were aligned and are shown in FIG. 1C.

The aligned repeats were identified as WD-40 repeats by application ofthe criteria identified in parts A, B and C above. For example, theconserved amino-terminal set in repeats I, II, III and V consists of thetypical “GH”, whereas in repeats IV, VI and VII, the set consists ofother residues. These other residues, however, are contained in at leastone of the amino acid groups identified above as conserved at theappropriate position. The conserved carboxyl-terminal set contains thehighly-conserved “D” at its first position in all repeats except repeatVI. The second-to-last position of this set contains the relatively-wellconserved “W” in each repeat, while the last position contains thetypical “D” in repeats II, V and VI, and other residues in the otherrepeats.

Taken together, these data indicate that the repeats contained in RACK1are WD-40 repeats. The data also illustrate that not all repeats containall of the elements typical of a WD-40 motif, but that when the repeatsare aligned and viewed together as a whole, a WD-40 motif is apparent inall repeats.

E. Identification of WD-40 Repeats in Sequenced Proteins

Data were compiled in support of the present invention to illustrate howWD-40 repeats in various proteins may be identified, and to illustratethe diversity of amino acid sequences that may be properly identified asWD-40 repeats by those skilled in the art following the guidance setforth herein. Two methods that were used to identify WD-40-containingprotein sequences are detailed in Example 7.

In the first method, proteins identified in their description as havinga homology to β-transducin were examined as detailed in parts B-D,above, for WD-40 repeats. 30 proteins were identified in this manner.The amino acid sequences of these proteins, with the WD-40 regionsaligned and delineated, are shown in FIGS. 12-18, 20-27, 29-30, 34-35,37-38, 40 and 42-50. The sequences are represented in the SequenceListing as SEQ ID NO:29-35, 37-44, 46-47, 51-52, 54-55, 57 and 59-67.

In the second method, proteins whose sequences were homologous to aconsensus WD-40 motif (SEQ ID NO:262), were identified and examined forWD-40 repeats. Ten additional proteins containing WD-40 repeats wereidentified with this strategy. The amino acid sequences of thoseproteins, with the WD-40 repeats aligned and delineated, are shown inFIGS. 11, 19, 28, 31-33, 36, 39, 41 and 51. The sequences arerepresented in the Sequence Listing as SEQ ID NO:28, 36, 45, 48-50, 53,56, 58 and 68.

Other types of searches may be equally effective at identifying proteinswhich may contain WD-40 repeats. For example, on-line databases such asGenBank or SwissProt can be searched, either with an entire sequence ofa WD-40-containing protein, or with a consensus WD-40 repeat sequence.Various search algorithms and/or programs may be used, including FASTA,BLAST or ENTREZ. FASTA and BLAST are available as a part of the GCGsequence analysis package (University of Wisconsin, Madison, Wis.).ENTREZ is available through the National Center for BiotechnologyInformation, National Library of Medicine, National Institutes ofHealth, Bethesda, Md.

Sequences identified with a protein homology search are then analyzed asdescribed in parts A, B and C, above, to identify potential WD-40motifs. Once located, the motifs can be aligned, and effective bindingpeptides may be designed.

F. Identification of WD-40 Regions in Novel Polypeptides

WD-40 repeats may be identified in a novel polypeptide by, for example,the methods described in parts A-D above. It will be appreciated,however, that step A above (homology matrix) is not required in theidentification of WD-40 repeats. Following the guidance of the presentinvention, one skilled in the art may, for instance, identify a WD-40motif while scanning the sequence of some, perhaps novel, polypeptidemerely through a recognition of one or more of the featurescharacteristic of WD-40 repeats.

The precise methods by which one skilled in the art arrives at theconclusion that a particular motif is a WD-40 repeat is less relevant tothe present invention than is the use of sequences derived from WD-40motifs, regardless of how they are identified, to design peptideseffective to alter or modulate the activity of one member of a pair ofinteracting proteins and/or to disrupt protein-protein interactions.

VI. Identification of Activity-altering Peptides

Upon the alignment and recognition of WD-40 repeats in a particularprotein, one may proceed to design a peptide or a set of peptides thatmay be effective to associate with or bind to the protein with which theWD-40-containing protein normally associates. Such a binding orassociation may be expected to alter or modulate the activity of theprotein and/or disrupt the association of the pair of interactingproteins.

The sequence of such a peptide will typically be homologous, if notidentical to, a contiguous amino acid sequence contained within at leastone of the WD-40 repeats. Examples of the selection of WD-40-derivedpeptides effective to disrupt protein-protein interactions are detailedin parts C and D below, for RACK-PKC and Gβ/γ-βARK interactions,respectively.

A. Choosing an Appropriate Region within a WD-40 Repeat

Putative binding peptides may be selected from any portion of a WD-40repeat. If it is desired to obtain a degree of discrimination betweenthe various WD-40-containing proteins, peptides should be chosen fromthe region between, and not including, the amino-terminal andcarboxyl-terminal conserved sets. This “central region” typically showsgreater sequence diversity between different WD-40-containing proteinsthan the terminal regions, and is roughly outlined by boxes in FIGS.11-51, which show the amino acid sequences and aligned WD-40 repeats ofvarious WD-40 repeat-containing proteins. Within the central region,peptides should be selected from sequences that have little or nohomology to any other known sequences, save the sequence(s) of theprotein(s) targeted for disruption.

For example, peptides rIII (SEQ ID NO:4, seven amino acids) and rVI (SEQID NO:7, eight amino acids), are identical to segments of RACK1 WD-40repeats (III and VI, respectively) beginning five amino acids in fromthe amino termini of the WD-40 repeats from which they are derived (seeFIG. 1C, underlined segments). The WD-40 repeat segments correspondingto the binding peptides comprise the left portion of the central regionof the respective WD-40 repeats, and are not well-conserved in RACK1.

If it is desired to inhibit the interactions of, for example, all of theisoforms of a particular WD-40-containing protein family, a sequences isselected that includes a significant number of residues that are sharedor highly homologous among at least one WD-40 repeat of each of thetargeted isoforms.

If, on the other hand, an isoform-specific reagent is desired, asequence is selected from a WD-40 repeat(s) of a specific isoform, wherethat sequence does not include a significant number of residues that areidentical or highly homologous to residues in WD-40 sequences fromrelated isoforms.

B. Choosing an Appropriate Length for a Peptide

Effective binding peptides may be designed that range in length from asfew as about four residues to 40 or more residues. Preferably, bindingpeptides will have a length of at least about six residues, and lessthan about 20 residues. The length will be determined in part by thedegree of desired homology to other WD-40 repeats, as described in partA above, and by the level of discrimination between proteins that isrequired.

For example, binding peptides selected from RACK1 sequences to inhibitRACK1/PKC interactions were seven and eight amino acids in length. Thepeptides are long enough to bind specifically to the targeted sequences,but short enough to not cross-react with other WD-40 repeat bindingproteins. These properties enable the peptides to have very selectiveand specific effects, as is shown below in Examples 6-11.

C. Design of RACK1 WD-40-derived Peptides to Inhibit RACK1-PKCInteractions

Peptides rIII (SEQ ID NO:4, seven amino acids) and rVI (SEQ ID NO:7,eight amino acids) were designed in part following the guidancepresented in parts A and B above. The peptides are identical to segmentsof RACK1 WD-40 repeat sequences beginning five amino acids in from theamino termini of the WD-40 repeats from which they are derived. TheWD-40 repeat segments corresponding to the binding peptides comprise theleft portion of the central region of the WD-40 repeats. The peptideswere tested for their ability to disrupt protein-protein interactions invitro and in vivo, as described in section VII and Examples 6-11 below.

D. Peptides Derived from WD-40 Repeats of Human G-Beta InhibitInteractions of G-Beta Subunits with βARK

Methods described in section V part E were used to identify WD-40repeats (SEQ ID NO:128-134) in Human G-Beta (SEQ ID NO:41). Segmentsfrom the first six WD-40 repeats were selected for the design of G-betabinding peptides (SEQ ID NO:13-18). The segments were selected based oncriteria detailed in parts A and B, above.

The G-beta binding peptides are used to disrupt the interactions ofG-beta subunits with LARK. The disruption is assayed using amodification of the overlay assay described in Example 4.

VII. Testing of Putative Binding Peptides

Detailed below are several assays by which the efficacy of WD-40-derivedpeptides at binding to a target protein, inhibiting protein-proteininteractions, and altering or modulating the activity of a targetprotein may be determined.

One class of assays, widely-used to assess the binding of two proteinsto each other, are overlay assays. Overlay assays are generallyapplicable to most proteins. They can be used to, for example, assessthe binding of WD-40-derived peptides to their targets, as shown inExample 6 and described in part B below. Overlay assays can also be usedto assess the ability of WD-40-derived peptides to inhibit the bindingof two interacting proteins, one of which contains a WD-40 motif fromwhich the peptides were derived (see, for instance, Example 4 and part Cbelow).

Other assays may be used to assess effects of WD-40-derived peptides onthe activity of the target protein. These assays may be in vivo assays,in vitro assays, or a combination of in vivo and in vitro assays. Theassay used will depend on the proteins involved and on the system(s)and/or process(es) that involve the interacting proteins against whichthe peptide was targeted. For instance, the assays described in partsD-I below are appropriate for characterizing PKC activity in vivo and invitro.

While many of the assays below are particularly useful forcharacterizing the activity of PKC, they also illustrate a generalframework of experiments by which the effects of WD-40 derived peptideson other proteins may be assessed.

A. Overlay Assays to Evaluate Efficacy of Putative Binding PeptidesDerived from WD-40 Regions

An overlay assay can be used to assess the disruption of the ability ofa pair of proteins to associate. Methods for conducting overlay assaysare well-known in the art (see, for example, Mochly-Rosen, et al.,1991).

Applications of overlay assays to evaluate putative binding peptides forPKC/RACK1 interactions are presented in Examples 4 and 5 herein. Theassays can be generally described as follows.

One protein of a pair of interacting proteins (“immobilized” protein)can be resolved on an SDS/PAGE gel and blotted onto an appropriatemembrane (for example, nitrocellulose or nylon) by methods known tothose skilled in the art. The blots may then be contacted with asolution containing the other protein of the pair of interactingproteins (“overlay” protein) in the presence, and in the absence ofputative binding peptides. Following appropriate wash steps, boundoverlay protein can be detected by the use of an appropriate probe, suchas an antibody directed against the overlay protein.

A variation on the above protocol may be performed to minimize apossible interference between unbound binding peptide and antibodiesused to detect the presence of bound overlay protein. The modificationconsists of performing another SDS/PAGE electrophoresis between thesteps of binding the overlay protein, and detecting the overlay proteinwith antibody or other probe. It is accomplished by cutting the blotinto pieces sized to just encompass the area occupied by the blottedimmobilized protein, after the overlay protein had been contacted (inthe presence or in the absence of binding peptides) and allowed to bindto the blot. The pieces of membrane are then incubated in a samplebuffer, placed in the wells of a second SDS polyacrylamide gel andsubjected to electrophoresis.

Following electrophoresis, the gel is blotted as above, and contactedwith a probe, for example antibodies, to detect bound overlay protein.

B. Binding of βPKC to Peptides Homologous to a WD-40 Region of RACK1

The binding of βPKC to peptide I (SEQ ID NO:1), peptide rVI (SEQ IDNO:7) and control peptide (SEQ ID NO:9) was assessed in Example 6 usinga PKC overlay assay similar to that described in Example 3. Increasingamounts of peptides were applied onto nitrocellulose using a slot-blotapparatus. The membranes were incubated with PKC in the presence andabsence of PS, DG, and calcium.

The data are shown in FIG. 4, and show that activated PKC bound to bothpeptides I and rVI at peptide amounts as low as 5 μmoles, but not to thecontrol peptide. Unactivated PKC did not bind to peptide I, but did bindto peptide rVI at similar concentrations.

The results indicate that while the peptides were homologous to oneanother and were capable of binding to the same protein, they behaveddifferently. Peptide rVI (SEQ ID NO:7; 8 residues) was able to bind toboth activated as well as unactivated forms of PKC, whereas peptide I(SEQ ID NO:1; 15 residues) could bind only to activated PKC. Thedifferences between the binding properties may be due, for example, tocharge differences and/or length differences between the two peptides.

C. Effects of Peptides Homologous to WD-40 Region of RACK1 on PKCBinding to RACK1

Two peptides (peptide rIII; SEQ ID NO:4 and peptide rVI; SEQ ID NO:7)identical to regions of RACK1 WD-40 repeats (underlined, FIG. 1C) weretested for their ability to inhibit PKC binding to recombinant RACK1using a modification of the overlay procedure referred to above. Theexperiment is detailed in Example 4 and the results are shown in FIG. 3.

Peptide I caused an 81±6% inhibition of PKC binding to recombinant RACK1as compared with binding in the absence of added peptide. Both peptidesrIII and rVI inhibited the binding of PKC to RACK1. In addition,peptides rI and rII were also effective inhibitors of the interaction ofPKC to RACK1. A lesser inhibitory effect was obtained with peptides rIVand rV and no inhibition was obtained with peptide rVII.

The difference in the peptide's ability to inhibit binding may reflectdifferences in the roles played by the corresponding WD-40 repeats inthe protein-protein interactions between PKC and RACK1. The peptide'sability or inability to inhibit protein-protein interactions as assayedby an overlay assay, however, is not necessarily correlated with theeffects those peptides may have on the activity of the targetedproteins, as measured by both in vivo and in vitro assays and describedin parts D-I below.

D. Effects of Peptides Homologous to WD-40 Regions of RACK1 onPKC-mediated Oocyte Maturation

Peptides I (SEQ ID NO:1), rIII (SEQ ID NO:4) and rVI (SEQ ID NO:7) werealso tested for their ability to affect insulin-induced, PKC-mediatedmaturation in Xenopus oocytes, as detailed in Example 7 and shown inFIGS. 5A and 5C.

PKC is involved in the maturation of Xenopus oocytes. Phorbol esters,which activate PKC, or microinjection of a constitutively active mutantof PKC induce the first stage of oocyte maturation in the absence ofhormones. Exposure to insulin causes an increase in diacylglycerollevels and microinjection of activated PKC enhances insulin-inducedmaturation (Stith, et al.). Microinjection of purified RACK proteinscauses a significant decrease in the rate of oocyte maturation (Smith,et al., 1992). The insulin-induced oocyte maturation assay thereforeprovides an effective in vivo assay for compounds that interfere withthe function of PKC.

The maturation response was quantified by monitoring the appearance of awhite spot in the animal hemisphere of the oocyte, indicating germinalvesicle breakdown (GVBD) and maturation. The indicated peptides weremicroinjected into Xenopus oocytes and the percent of oocytes with GVBDfollowing insulin exposure was plotted as a function of time in FIGS. 5Aand C.

Approximately 80-85% of sham-injected (control) oocytes exposed toinsulin reach maturation, as compared with 45-50% of oocytes injectedwith peptide I. The rate of maturation of those oocytes that did maturewas similar in the two cases. In contrast the effects of peptide I, bothpeptides rIII and rVI potentiated the effects of insulin on oocytematuration, both in terms of the rate of maturation, and in the totalfraction of oocytes that mature during the experiment. Injection ofpeptides rIII or rVI increases the fraction of maturing oocytes toessentially 100%. Furthermore, peptide rVI induced oocyte maturation inthe absence of insulin stimulation (FIG. 5B).

Together, the data above indicate that peptides homologous to the WD-40region of RACK1 can modulate the function of a protein with which RACK1interacts (e.g. PKC), that the modulation can occur in vivo, and that itcan have clear and profound physiological consequences. Furthermore, theresults with peptide rVI suggest that under appropriate circumstances,the peptide alone may act to activate PKC, in the absence of otheractivating substances.

E. Effects of Peptides Homologous to WD-40 Regions of RACK1 on PKCTranslocation in Xenopus oocytes

Insulin causes the redistribution of βPKC, but not other PKC isozymes,from a cytosolic form to a membrane-associated form, as evidenced by therelative levels of PKC in the soluble vs. the particulate fraction ofoocyte homogenate. To assess the effects of RACK1 WD-40-derived peptideson insulin-induced PKC translocation, 50 nl of a 20 mM NaCl solutioncontaining the indicated peptides were microinjected into Xenopusoocytes. The oocytes were then homogenized, and the relative amount ofPKC in the soluble and particulate fractions was assayed. The protocolfollowed was a modification of a method described by Smith, et al(1992). The results are shown in FIG. 6.

Peptide I (50 μM) did not affect βPKC distribution in untreated oocytes,but inhibited insulin-induced βPKC translocation (FIG. 3, lanes 7,8). Incontrast, peptide rVI (50 μM) induced βPKC translocation in the absenceof insulin treatment (FIG. 3, lanes 3,4). These results suggest thatpeptide I is an antagonist of hormone-induced PKC translocation, whereaspeptide rVI is an agonist and an activator of PKC translocation. Inlight of the results presented in Example 7, the data also suggest thatthe inhibition of insulin-induced GVBD following microinjection ofpeptide I was due to an inhibition of βPKC translocation.

F. Effects of Peptides Homologous to WD-40 Regions of RACK1 onSensitivity of βPKC to Arg-C Endopeptidase

Upon activation of PKC, a pseudosubstrate autoinhibitory sequence at theN-terminus of PKC dissociates from the catalytic site and renders themolecule sensitive to endopeptidase Arg-C (Orr, et al.). Exposure ofactivated βPKC to Arg-C results in a limited proteolysis, or “nicking”of the enzyme. The nicking typically generates a 78 kDa fragment andseveral small fragments. Continued exposure to Arg-C typically resultsin the disappearance of βPKC (Orr, et al.).

Since peptides rIII (SEQ ID NO:4) and rVI (SEQ ID NO:7) exhibited PKCagonist activities in other assays (see, for instance Examples 7 and 8),experiments were performed to determine whether the peptides werecapable of activating PKC in a manner to make it susceptible toendopeptidase Arg-C. The experiments are detailed in Example 9 and theresults are shown in FIG. 7.

In the presence of effective concentrations of PKC activators (0.8 μg/mlDG, 50 μg/ml PS and 1 mM CaCl₂), exposure of βPKC to Arg-C resulted innicking, generating the 78 kDa fragment (FIG. 7, lane 2). In the absenceof PKC activators, exposure of βPKC (80 kDa) to endopeptidase Arg-C hadno effect on the enzyme (FIG. 7, lane 1).

Incubation of βPKC with Arg-C at low concentrations of activators (2.5μg/ml PS and 50 μM CaCl₂) in the absence of added peptide, in thepresence of control peptide (SEQ ID NO:9) and in the presence of peptideI (SEQ ID NO:1) did not result in appreciable nicking activity (FIG. 7,lanes 4, 8 and 9, respectively). However, incubation of βPKC with thesame low concentration of activators in the presence of peptides rIII orrVI resulted in the appearance of the 78 kDa nicked PKC fragment(effects of peptide rVI in FIG. 4, lanes 5-7). Concentrations as low as10 nM of peptide rVI were sufficient to result in nicking activity,indicative of βPKC activation.

The results indicate that peptides rIII and rVI, but not peptide I, areeffective to stabilize PKC in an activated conformation that renders itsusceptible to Arg-C under conditions of low PKC activators that wouldotherwise not render the enzyme susceptible to Arg-C.

G. Effects of Peptides Homologous to WD-40 Regions of RACK1 on βPKCAutophosphorylation

Activated PKC is capable of autophosphorylation, which can be assayed byincubation with [γ-³²P] ATP and visualized on an autoradiograph of agel. Anti-pseudosubstrate antibodies were shown previously to induceautophosphorylation in the absence of PKC activators (Makowske, et al.).Since peptide rVI (SEQ ID NO:7) was effective to induce PKCtranslocation and GVBD in the absence of PKC activators, experimentswere performed to determine if the peptide was also capable of inducingPKC autophosphorylation. The experiments are detailed in Example 10 andthe data are shown in FIG. 8.

PKC activated with PS (50 μg/ml), DG (0.8 μg/ml) and CaCl₂ (1 mM) showsnormal levels of autophosphorylation (lane 1). No autophosphorylationwas seen in the absence of PKC activators (lane 2), or in the absence ofPKC activators with peptide I (SEQ ID NO:1; lane 5) or control peptide(SEQ ID NO:9; lane 6). In contrast, peptide rVI in the absence of PKCactivators induced PKC autophosphorylation to over 80% of the levelsobtained for PKC alone in the presence of optimal concentration of PS,DG, and calcium (compare FIG. 8 lane 1 (control) with lane 4 (peptiderVI)).

H. Effects of Peptides Homologous to WD-40 Regions of RACK1 on HistonePhosphorylation by βPKC

Another measure of PKC activity is the ability of activated PKC enzymeto phosphorylate histones. PKC phosphorylation of histone was carriedout using a modification of the protocol described by Mochly-Rosen, etal., (1987). Phosphorylation was carried out in the presence or absenceof PKC activators (PS, DG and calcium) and RACK1-derived peptides.Phosphorylated histone was detected by autoradiography, followingSDS-PAGE on a 10% gel.

Since peptide rVI (SEQ ID NO:7) was effective to induce theautophosphorylation of PKC in the absence of PKC activators, and bothpeptides rIII (SEQ ID NO:4) and rVI rendered PKC susceptible toproteolysis by Arg-C, experiments were performed to characterize theeffect of the peptides on histone type III phosphorylation by PKC. Theexperiments are detailed in Example 11 and the results are shown inFIGS. 9 and 10.

The results are similar to those obtained for the effects of peptide rVIon autophosphorylation of PKC, that is, peptide rVI was effective toinduce PKC-mediated histone phosphorylation in the absence of the PKCactivators PS, DG, and calcium, once again supporting that peptide rVIis an agonist of PKC activation. Peptide rIII similarly induced histonephosphorylation (FIG. 10).

VIII. Utility

A. Peptides as Probes for the Identification of Target Proteins

WD-40 derived peptides may be used, for example, to isolate clonesencoding target proteins from an expression library. Variations on thecloning methods described herein can be used to identify clonesexpressing sequences capable of binding the peptides. For example, WD-40derived peptides may be used to detect a target protein on a membraneusing a standard binding assay. Positive clones may be detected, forexample, by radiolabeling the peptides and exposing the membrane tofilm.

Target proteins isolated in this manner may be completely novel, or theymay be partially characterized (in terms of a biological activity in ahomogenate, or a band on a protein gel, for example).

Upon isolation of a cDNA encoding a binding protein, the cDNA may beexpressed, for example, as detailed herein, and the protein may becharacterized. Purified protein thus isolated may be used for a numberof applications, including the production of antibodies.

Peptides designed according a method of the present invention may alsobe used, for example, as probes in a Western blot of a tissue homogenateto identify and determine the molecular weight of known or putativetarget proteins.

Screens such as those described above may be facilitated by themodification of peptides used for screening to incorporate any of avariety of reporter moieties. For example, the peptides can beradiolabeled with ¹²⁵I. Alternatively, the peptides can be modified witha sequence-tag or a ligand for an affinity column by methods known tothose skilled in the art.

The peptides may also be modified to covalently cross-link to theirtargets after binding, for example with any of various affinity reagentfor cross linking known to those skilled in the art. This enables theisolation of target proteins that bind the peptides relatively weakly.

B. Peptides as Substitutes for Defective WD-40 Containing Proteins

In cases where a WD-40 containing protein is implicated in a disease(see, for example Reiner, et al.), peptides derived from WD-40 regionsof the defective protein may be used as substitutes, for example, toactivate a target enzyme. Such an approach may be more feasible thanattempting therapy with intact proteins. The approach has an additionaladvantage in that it does not require knowledge of the chromosomallocation of the affected gene.

The peptides can be introduced into affected cells by any of severalmethods known to those skilled in the art, including through the use ofan appropriate expression vector or through in vitro synthesis andadministration by an effective, expedient route. In vitro studies can becarried out using skinning or microinjection techniques.

C. Peptides as Pharmaceutical Agents

WD-40 derived peptides of the present invention may be usedtherapeutically, as described above. Such peptides may be designed so asto interact with endogenous target molecules to augment or correct theirfunction. Alternatively, peptides may be designed to specificallyinteract with target molecules unique to a pathogenic organism.

D. Peptides as Modulators of Enzyme Activity of Proteins Involved inProtein-protein Interactions

Peptides synthesized according to a method of the invention may beeffective to modulate the function of a target molecule (e.g. serve asagonists or antagonists). As shown herein, for example, peptides rVIIIand rVI can serve to activate or enhance the activation of PKC, whereaspeptide I can inhibit PKC.

These activities may be used in screens to identify other compoundswhich may affect the function of target molecules such as PKC. Inparticular, because WD-40 derived peptides may interact with PKC in amanner that is more similar to in vivo interactions (i.e. proteinbinding), they may be useful for identifying molecules or compounds thatmay interfere with PKC function in vivo, but might not necessarilyinterfere with PKC in vitro.

For example, peptide rVI can be used to stimulate PKC in the absence oftraditional PKC activators, and the rVI-stimulated enzyme may be used ina screen to identify, for example, novel PKC-inhibiting orPKC-potentiating compounds.

If constitutive activation or inactivation of a target enzyme isdesired, peptides may be designed with integrated or derivatizedcross-linking moieties. The peptides can be cross-linked to theirtargets upon binding such that the target molecule assumes the desiredstate of activity for the lifetime of the target molecule.

Conversely, as described herein for PKC, peptides may also be designedso as to accelerate the degradation of the target molecule. For example,peptide rIII accelerated the degradation of PKC in cardiac myocytes.

E. WD-40 Derived Peptides as Specific Modulators of Isozymes

Peptides designed according to a method of the present invention canalso be used to provide target isozyme-specific modulator molecules. Forexample, most cells have several PKC isozymes, all of which areactivated by the same cellular stimuli. Determining the function of theindividual isozymes is therefore difficult.

WD-40 derived peptides that selectively stimulate or inhibit specifictarget isozymes or groups of isozymes may be useful, both in terms oftherapeutic value, and in terms of determining the roles of differentisozymes in cellular function and disease. Such information can beuseful for the identification of new molecular targets for drugdevelopment, as is described in part F, below.

F. Compounds Designed Based on the Predicted Structure of BindingPeptides as Pharmaceutical Agents

Peptides derived from WD-40 repeats may be useful for identifying leadcompounds for drug development. Peptides as small as 7 residues havebeen shown herein to possess specific bioactivities upon interactionwith their targets in vivo. The structure of such small peptides can bereadily determined by a number of methods, such as NMR and X-raycrystallography. A comparison of the structures of peptides similar insequence, but differing in the biological activities they elicit in thetarget molecules, can provide information about the structure-activityrelationship (SAR) of the target enzyme.

For example, peptide I and RACK1-derived peptides rIII (SEQ ID NO:4) andrVI (SEQ ID NO:7) had opposite effect in vivo, although they arehomologous in sequence.

Information gleaned from the examination of structure-activityrelationships can be used to design either modified peptides, or othersmall molecules or lead compounds which can be tested for predictedproperties (e.g. agonist or antagonist), as related to the targetenzyme. The activity of the lead compounds can be evaluated using assayssimilar to those used in the evaluation of peptide-binding effects.

Information relating to a SAR of a target enzyme may also be obtainedfrom co-crystallization studies. In such studies, a peptide with adesired activity is crystallized in association with a target protein,and the X-ray structure of the complex is determined. The structure canthen be compared, for example, to the structure of the target protein inits native state, and information from such a comparison may be used todesign compounds expected to possess specific activities. The compoundscan be evaluated using assays similar to those used in the evaluation ofpeptide-binding effects.

G. PCR of cDNA Corresponding to WD-40 Repeats to Identify Mutations inWD-40 Containing Proteins

Results presented herein suggest that the middle regions of WD-40 motifsare involved in the association of a WD-40 protein with its targetprotein. Because this association is likely to play a central role inthe activity of a polypeptide complex comprised of interacting proteins,some genetic diseases may include mutations at these regions of WD-40containing proteins. Therefore, if a WD-40 containing protein isimplicated in a genetic disorder, it may be possible to use PCR toamplify DNA from the WD-40 regions to quickly check if a mutation iscontained within one of the WD-40 motifs. Primers can be madecorresponding to either (i) the flanking regions of each repeat or (ii)the flanking regions of a series of tandem repeats from the affectedgene. Standard sequencing techniques can be used to determine whether amutation is present. This method does not require prior chromosomemapping of the affected gene and can save time by obviating the need tosequence the entire gene encoding a defective WD-40 protein.

H. WD-40 Based Polypeptides as Affinity Ligands

Since the polypeptide compositions of the invention are able to bindproteins of interest, generically called a “first protein”, thepolypeptide compositions can also be used to retrieve the proteins ofinterest from samples and the peptides can be used as affinity ligandsfor chromatographic procedures to purify and analyze said proteins.Standard chromatographic techniques are employed. Typically, thepolypeptide is coupled to a solid support and the sample putativelycontaining the first protein is contacted with the polypeptidecomposition of the invention; any unbound components of the sample areremoved and, if desired, the first protein, bound to support, is elutedand recovered.

I. Use of Peptides in Screening Tests for Candidates

Various candidate compounds, not necessarily polypeptides, may be shownto bind to a first protein using the polypeptides of the invention ascompetitors. In these screening assays, the ability of a candidatecompound to bind a first protein can be assessed by contacting the firstprotein with the polypeptide composition of the invention in thepresence and absence of the candidate compound and evaluating the levelof binding of the polypeptide in the presence as opposed to the absenceof the candidate. Decreased binding of the polypeptide in the presenceof the candidate indicates that the candidate binds to the firstprotein.

More broadly, the interaction of a protein with a polypeptidesubsequence contained in the second protein can be assessed bycontacting the first protein with a polypeptide representing thesubsequence and observing any interaction with the polypeptidecomposition.

IX. Production of the Peptides of the Invention

The polypeptides of the invention can be prepared using standardtechniques for the synthesis of peptides from amino acids. Suchtechniques, when conducted in solid phase chemistry are availablecommercially.

The polypeptides of the invention may also be produced using recombinantmethods. These methods are by now well known in the art; DNA moleculescontaining nucleotide sequences encoding the desired polypeptides canreadily be synthesized and ligated into expression systems forproduction of the peptides as is understood in the art. A wide varietyof hosts is available, including procaryotic and eucuryatic hosts. Theconstruction of expression vectors, means to modify these hosts, andculturing the modified hosts for recombinant production of polypeptidesare conducted using standard techniques.

The following examples illustrate, but do not limit the presentinvention.

Materials and Methods

Nitrocellulose filters were obtained from Schleicher and Schuell (Keene,N.H.).

Synthetic peptides were prepared using commercially available automatedpeptide synthesizers. Alternatively, custom designed peptides may bepurchased, for example, from Bachem Bioscience (King of Prussia, Pa.).Peptides may also be prepared recombinantly by expressingoligonucleotide sequences encoding the peptides. The oligonucleotidesequences may be either synthesized directly by standard methods ofoligonucleotide synthesis, or, in the case of large coding sequences,synthesized by a series of cloning steps involving a tandem array ofmultiple oligonucleotide fragments corresponding to the coding sequence(Crea; Yoshio, et al.; Eaton, et al.). Oligonucleotide coding sequencescan be expressed by standard recombinant procedures (Maniatis, et al.;Ausubel, et al.).

“Triton” refers to a nonionic detergent comprising a polyoxyethyleneether and other surface-active compounds. An exemplary Triton detergentis “TRITON X-100”, available from Sigma Chemical Company, St. Louis, Mo.

“Tween” refers to a nonionic detergent comprisingpolyoxyethylenesorbitan monolaurate with a fatty acid composition ofapproximately 55% lauric acid, with a balance composed primarily ofmyristic, palmitic and stearic acids. An exemplary Tween detergent is“TWEEN 20”, available from Sigma Chemical Company, St. Louis, Mo.

“SDS” refers to sodium dodecyl sulfate.

“PAGE” refers to polyacrylamide gel electrophoresis.

“IPTG” refers to isopropyl β-D-thiogalactopyranoside.

EXAMPLE 1 Expression Cloning of a PKC-binding Protein

A. Buffers

Overlay block buffer: 50 mM Tris-HCl (pH 7.5), 0.2 M NaCl, 3% bovineserum albumin (BSA) and 0.1% polyethylene glycol.

Overlay buffer: 50 mM Tris-HCl (pH 7.5), 0.2 M NaCl, 12 mM2-mercaptoethanol, 0.1% BSA, 1% polyethylene glycol, 10 μg per mlsoybean trypsin inhibitor and 10 μg per ml leupeptin.

B. Isolation of a PKC-binding cDNA Clone by an Overlay Assay

A rat brain (Sprague Dawley) cDNA expression library, constructed in thelambda phage cloning vector “UNI-ZAP XR” (Stratagene, La Jolla, Calif.),was screened by an overlay assay as follows.

Lifts of nitrocellulose filters from IPTG-induced cDNA library plateswere incubated for 2 hours in overlay block buffer. The filters werethen transferred to overlay buffer with or without 1 unit of a mixtureof rat brain PKC isozymes (α, β, γ, δ, ε and ζ, ˜10 nM finalconcentration each) and incubated for 20 minutes at room temperaturewith PKC activators (60 μg/ml phosphatidylserine (PS), 2 μg/mldiacylglycerol (DG), 1 mM CaCl₂)

Following three 15 minute washes in the overlay buffer, the filters wereincubated in the overlay block buffer in the presence of a mixture ofmonoclonal anti-α, β and γ PKC antibodies (1:1000 dilution; SeikagakuKogyo, Tokyo, Japan) and polyclonal anti-δ, ε and ζ PKC antibodies(1:500 dilution; Life Technologies, Gaithersburg, Md.). After a 16 hrincubation at room temperature, the filters were washed three times, 15minutes per wash, in overlay buffer.

Binding of PKC was determined using alkaline phosphatase-conjugated goatanti-rabbit or goat anti-mouse antibodies (1:2000 dilution, BoehringerMannheim Biochemicals, Indianapolis, Ind.). The alkaline phosphatasereaction used 5-bromo-4-chloro-3-indoyl phosphate p-toluidine salt as asubstrate, and was performed following the manufacturer's protocol.

Library screening of 2.4×10⁶ recombinant “UNI-ZAP” lambda phage plaquesyielded one clone, pRACK1, that reacted with anti-PKC antibodies in thePKC overlay membrane, but not in the control overlay membrane. Theseresults suggest that pRACK1 encodes a PKC binding protein.

C. Cloning and Sequencing cDNA from Positive Plaques

The clone pRACK1, identified as detailed in part B above, was plaquepurified and cDNA inserts were isolated as phagemids by in vivo excisionof the cloning vector, according to the manufacture's protocol(Stratagene, La Jolla, Calif.). DNA sequencing of pRACK1 was carried outusing standard di-deoxy sequencing techniques (Maniatis, et al.) The DNAsequence of RACK1 is shown in FIG. 1A. The sequence is also contained inthe Sequence Listing as SEQ ID NO:19.

EXAMPLE 2 Expression and Purification of Recombinant RACK1 Protein in E.coli

A PstI/XhoI DNA fragment containing an open reading frame of 317 aminoacids from the putative translation start site of pRACK1 (see underlinedATG in FIG. 1A) and 8 additional nucleotides upstream of the initiatingmethionine was subcloned into E. coli expression vector pMAL-c2 (NewEngland BioLabs, Beverly, Mass.). This vector contains the malE gene,which encodes maltose-binding protein (MBP). Induction of E. colicontaining the vector results in the production of an MBP-fusion protein(Ausubel, et al.). The vector also includes a recognition site for theprotease factor Xa, which allows the protein of interest to be cleavedfrom MBP after purification without adding any vector-derived residuesto the protein.

A culture of TB1 E. coli transformed with RACK1-containing pMAL-c2 wasinduced by a 3 hr incubation with 1.8 mM IPTG. A protein fractioncontaining a 78 kDa fusion protein, comprised of RACK1 fused to MBP wasisolated from the cultured E. coli by standard methods (Ausubel). Thefusion protein was purified on an amylose affinity column according tothe manufacture's protocol (New England BioLabs, Beverly, Mass.) andincubated with protease Xa (New England BioLabs) to yield a 36 kDaprotein (RACK1) and a 34 kDa protein (possibly a RACK1 degradationproduct).

EXAMPLE 3 Binding of PKC to Recombinant RACK1

A. Buffers

PBS/Tween buffer: 140 mM NaCl, 8 mM Na₂PO₄, 1.5 mM KH₂PO₄, 3 mM KCl and0.05% Tween at pH 7.0.

Overlay wash buffer: 50 mM Tris-HCl (pH 7.5), 0.2 M NaCl, 12 mM2-mercaptoethanol, 0.1% polyethylene glycol and 0.1 mM CaCl₂.

B. Overlay Assay

Purified recombinant RACK1 protein (100-250 μg per lane, produced asdetailed in Example 2) was subjected to SDS/PAGE and blotted ontonitrocellulose membranes (Ausubel). The nitrocellulose membranes werecut into strips, which were incubated for 0.5 hr in overlay buffer(Example 1) in the presence or absence of a mixture of PKC isozymes (α,β, γ, δ, ε and ζ, ˜10 nM each final concentration) and PKC activators(60 μg/ml phosphatidylserine (PS), 2 μg/ml diacylglycerol (DG), and 1 mMCaCl₂). Unbound material was removed by five washes, 5-min each, inoverlay wash buffer. Where indicated, PKC activators were present duringthe incubation of PKC with the nitrocellulose strips. The conditions foreach sample and corresponding results are presented in part D below.

C. Detection of Bound PKC

PKC bound to RACK1 immobilized on nitrocellulose strips was detected asfollows. The strips were incubated for 16 hours at room temperature witha mixture of anti-PKC antibodies as detailed in part B of Example 1, andthen washed three times, 15 minutes per wash, with PBS/Tween buffer. Thestrips were incubated with anti-mouse and anti-rabbit horseradishperoxidase-linked secondary antibodies (Amersham Life Science, ArlingtonHeights, Ill.) diluted 1:1000 in PBS/Tween buffer supplements with 2%BSA, for 1 hour at room temperature. After washing three times, 15minutes per wash with PBS/Tween buffer, the strips were subjected to achemiluminescent reaction with luminol (diacylhydrazide) as detailed inthe manufacturer's protocol (Amersham Life Science, Arlington Heights,Ill.), followed by an immediate exposure to autoradiography film(Eastman Kodak, Rochester, N.Y.) for 30 seconds to 5 minutes.

D. Effects of PKC Activation on PKC Binding to RACK1

The results presented in FIG. 2 show the influence of PKC activators onthe binding of PKC to RACK1 immobilized on nitrocellulose membranes. Theoverlay assay was carried out as described in part B above. The testreagents contained in each sample and the corresponding lanes on theblot presented in FIG. 2 are as follows. Lane 1: PKC, 60 μg/ml PS, 2μg/ml DG and 1 mM CaCl₂; lane 2: PKC and 1 mM EGTA; lane 3: PKC, 60μg/ml PS and 2 μg/ml DG; lane 4: PKC and 1 mM CaCl₂; lane 5: No PKCadded; lanes 6 and 7: PKC, 60 μg/ml PS 2 μg/ml DG, 1 mM CaCl₂, and 10 μMsubstrate peptide (SEQ ID NO:11; lane 6) or 10 μM pseudosubstratepeptide (SEQ ID NO:12; lane 7). The results are representative of threeindependent experiments.

It can be appreciated that the binding of PKC as detected by anti-PKCantibodies is minimal in the presence of EGTA or calcium alone (FIG. 2,lanes 2, 4, respectively), is greater in the presence ofphosphatidylserine (PS) and diacylglycerol (DG; lane 3), and is maximalin the presence PS, DG and calcium (lane 1). Antibody binding was notobserved in the absence of added PKC (lane 5). Furthermore, maltosebinding protein alone, or an extract from non-transformed E. coli didnot bind PKC.

The concentration dependence of PKC binding to RACK1 was characterizedwith βPKC, since this isozyme is a major component of the PKC mixtureused for the overlay assay. The mean half maximal binding was ˜0.375 nM,and maximal binding was ˜4 nM (n=3; values reflect binding of βPKCisozyme in the presence of other PKC isozymes and was determined byscanning autoradiograms in the linear range of detection, as describedin Mochly-Rosen, et al., (1991).

The results presented above indicate that in order for PKC to bind toRACK1 it must be activated. In vitro, activation may be accomplished,for example, by phosphatidylserine and diacylglycerol, or, morepreferably, by phosphatidylserine, diacylglycerol and calcium.

EXAMPLE 4 Inhibition of PKC Binding to RACK1 by RACK1-specificWD-40-homologous Peptides

Assays for the inhibition of PKC binding to RACK1 by putative bindingpeptides were carried out by combining a variation of the overlayprotocol described in Example 3 part B above, with an overlay extractionassay described in part B below. The variation in the overlay protocolconsisted of incubating the putative binding peptides with a mixture ofPKC isozymes for 15 minutes at room temperature before the mixture wasused to contact the nitrocellulose strips containing immobilized RACK1.

A. Buffers

Sample buffer: 0.3 M Tris HCl, 5% SDS, 50% glycerol, 0.01% bromophenolblue and 5% β-mercaptoethanol.

B. Overlay Extraction Protocol

Nitrocellulose strips containing immobilized RACK1, that had beencontacted with a solution containing a mixture of PKC isozymes, werewashed and the area corresponding to the 36 kDa (RACK1-containing) bandwas cut out. The pieces (containing PKC/RACK1 complexes) were incubatedwith sample buffer for 10 minutes at 80° C. The sample buffer and thenitrocellulose pieces were then placed in wells in the PAGE gel andsubjected to SDS-PAGE to elute the bound proteins. The gel was blottedonto nitrocellulose and a Western blot analysis was carried out usingthe mixture of antibodies (specific for PKC α, β, γ, δ, ε and ζisozymes) described in Example 1 part B. Bound antibodies were detectedby ¹²³I-protein A.

C. PKC Overlay in the Presence of Binding Peptides

Peptides derived from or homologous to WD-40 repeats of RACK1 weretested for their ability to inhibit PKC binding to recombinant RACK1.Binding of PKC to RACK1 was carried out using a variation of the overlayprocedure described in Example 3 part B. In the experimental samples,peptides were incubated with a solution containing a mixture of ratbrain PKC isozymes (˜10 nM each) for 15 minutes at room temperature.

Following completion of the modified overlay protocol, the samples weresubjected to the overlay-extraction protocol detailed in part B, above.

The results in FIG. 3 show the binding of PKC to RACK1, carried outwithout (lane 1) or with (lanes 2-4) a preincubation of peptides withPKC. Lane 2 shows PKC binding following a preincubation with 10 μMpeptide I (SEQ ID NO:1). Peptide I caused an 81±6% inhibition of PKCbinding to recombinant RACK1 as compared with binding in the absence ofadded peptide (n=3). Lanes 3 and 4 show PKC binding following apreincubation with 10 μM peptide rIII (SEQ ID NO:4) and 10 μM peptiderVI (SEQ ID NO:7), respectively. Both peptides inhibit the binding ofPKC to RACK1. It can be seen that peptide rIII is somewhat moreeffective than peptide rVI. The results shown are representative ofthree independent experiments.

The overlay-extraction method (part B above) was used in experimentsrelating to the peptide inhibition of PKC binding in order to decreasethe possibility that some part of the inhibition of PKC binding to RACK1reflects an interference in the binding of anti-PKC antibodies to thePKC/RACK1 complexes. Free peptides are effectively removed from thePKC/RACK1 complexes during the second round of SDS/PAGE, prior toblotting and detection of immobilized PKC/RACK1 complexes by anti-PKCantibodies.

EXAMPLE 5 Identification of Sequenced Proteins Containing WD-40 Repeats

A search for WD-40 motif-containing proteins was done using the ENTREZprogram, release 6.0 (National Center for Biotechnology Information,National Library of Medicine, National Institutes of Health, Bethesda,Md.). The ENTREZ database was searched for protein sequences related tothe β subunit of transducin.

Protein sequences homologous to β-transducin were examined for theexistence of WD-40 repeats, following the guidance for identification ofWD-40 repeats presented in section V of the specification, above.

The proteins were also used to carry out additional searches of thedatabase, in order to identify other proteins which may contain WD-40repeats, but which might not be homologous to the β subunit oftransducin. Sequences identified during the second round of searcheswere again examined for WD-40 repeats.

This search strategy identified 30 proteins containing WD-40 sequences.The amino acid sequences of these proteins, with the WD-40 regionsaligned and delineated, are shown in FIGS. 12-18, 20-27, 29-30, 34-35,37-38, 40 and 42-50. The sequences are represented in the SequenceListing as SEQ ID NO:29-35, 37-44, 46-47, 51-52, 54-55, 57 and 59-67. Anexamination of the sequences in the figures reveals that although therecan be divergence between the WD-40 motifs of different proteins, aconsistent pattern can be inferred based on the teachings presented inpart V of the specification above.

An additional search, using a consensus WD-40 sequence (SEQ ID NO:262),was conducted with the “MACVECTOR” program (Eastman Kodak Co., NewHaven, Conn.) to search GenBank (December 1993 release). Defaultsettings (matrix=250) were used for the search. The search identifiedthe 250 proteins with the highest homology to the consensus sequence.These proteins were examined, as detailed in part V above, for WD-40repeats. Ten additional proteins containing WD-40 repeats wereidentified with this strategy. The amino acid sequences of thoseproteins, with the WD-40 repeats aligned and delineated, are shown inFIGS. 11, 19, 28, 31-33, 36, 39, 41 and 51. The sequences arerepresented in the Sequence Listing as SEQ ID NO:28, 36, 45, 48-50, 53,56, 58 and 68.

EXAMPLE 6 Binding of βPKC to RACK1 WD-40-derived Peptides

A. Buffers

Peptide overlay block buffer: 20 mM Tris-HCl (pH 7.5), 0.2 M NaCl, 3%bovine serum albumin (BSA) and 0.1% polyethylene glycol.

Overlay wash buffer: 50 mM Tris-HCl (pH 7.5), 0.2 M NaCl, 12 mM2-mercaptoethanol, 0.1% polyethylene glycol and 0.1 mM CaCl₂.

B. PKC Overlay of Immobilized Peptides

The binding of βPKC to peptide I (SEQ ID NO:1), peptide rVI (SEQ IDNO:7) and control peptide (SEQ ID NO:9) was assessed using a PKC overlayassay similar to that described in Example 3. Increasing amounts ofpeptides (0.5 μmole, 1.0 μmole, 5.0 μmole and 10.0 μmole) suspended in20 mM NaCl were applied individually onto nitrocellulose using aslot-blot apparatus (Schleicher and Schuell, Keene, N.H.). Thenitrocellulose membrane was washed three times, 15 minutes per wash, inpeptide overlay buffer and incubated for two hours in peptide overlayblock buffer. The membrane was cut into sections and the sections weretransferred to different PKC-containing solutions and incubated for 30minutes at room temperature. All the solutions contained 5 nM rat brainPKC in peptide overlay buffer. Some solutions additionally contained PS,DG, and calcium. The membranes were then washed three times, 15 minutesper wash, in peptide overlay buffer and incubated in peptide overlayblock buffer containing anti-βPKC monoclonal antibodies (1:1000dilution; Seikagaku Kogyo, Tokyo, Japan). After a 16 hr incubation atroom temperature, the filters were washed three times, 15 minutes perwash, in peptide overlay buffer.

Binding of PKC was determined using chemiluminescence as described inExample 3, part C. Quantitation of PKC binding was carried out using a“MICRO SCAN” 1000 gel analyzer (Galai Inc., Yokneam, Israel).

The data show that activated PKC bound to both peptides I and rVI, butnot to the control peptide, at peptide amounts as low as 5 μmoles.Unactivated PKC did not bind to peptide I, but did bind to peptide rVIat similar concentrations.

The results indicate that peptide rVI is capable of binding bothactivated as well as unactivated forms of PKC, whereas peptide I bindsonly to activated PKC.

EXAMPLE 7 Effects of RACK1 WD-40-derived Peptides on PKC-mediated OocyteMaturation

Exposure to insulin induces maturation in Xenopus oocytes via aPKC-dependent pathway (Smith, et al., 1992). The maturation response maybe quantified by monitoring the appearance of a white spot in the animalhemisphere of the oocyte, indicating germinal vesicle breakdown (GVBD)and maturation. To assess the effects of RACK1 WD-40-derived peptides oninsulin-induced PKC-mediated maturation, 50 nl of a 20 mM NaCl solutioncontaining the indicated peptides [peptide I (SEQ ID NO:1; ), peptiderVI (SEQ ID NO:7; ▪), or injection solution (□)] (peptides at 50 μM)were microinjected into Xenopus oocytes. The symbols refer to symbolsused in FIG. 5, which shows the data from this example. One hourfollowing the peptide injections, the oocytes were exposed to a solutioncontaining insulin (8.25 μg/ml) for 2 minutes (t=0). 10-15 oocytes wereused for each sample.

The data, representative of three independent experiments, are expressedas the percent of oocytes with GVBD following insulin exposure and areplotted as a function of time in FIG. 5.

In oocytes injected with buffer or control peptide, onset of maturationwas typically 4-5 hours after exposure to insulin. Following this delay,%GVBD followed an approximately exponential time-course, reaching aplateau of about 85-90% GVBD at about 10-12 hours. These data indicatethat approximately 80-85% of sham-injected oocytes exposed to insulin att=0 reach maturation, and that maturation is reached relatively quickly(within about 10 hours) relative to the time-course of the experiment(20 hours).

Oocytes injected with peptide I (SEQ ID NO:1) responded in a mannersimilar to control oocytes, except the plateau was at about 45-50% GVBD.These data suggest that injection of peptide I blocked maturation inapproximately 40-45% of oocytes that would normally proceed tomaturation, but had little effect on the kinetics or extent ofmaturation of the remaining (50-55%) oocytes.

Oocytes injected with peptide rVI (SEQ ID NO:7) responded with aslightly shorter delay (about 3-4 hours), but reached a higher plateau(about 95-100% GVBD) more quickly (within about 5 hours) than controloocytes. These data suggest that peptide rVI potentiates the effects ofinsulin on oocyte maturation, both in terms of the rate of maturation,and in the total fraction of oocytes that mature during the experiment.Injection of peptide rVI increases the maturing fraction to essentially100%.

The effects of both peptides I and rVI on GVBD were dose-dependentbetween 5 μm-500 μM.

Since peptide rVI enhanced insulin-induced GVBD, experiments wereperformed to determine whether peptide rVI can induce GVBD in theabsence of insulin. The data from these experiments are shown in FIG.5B. Microinjection of peptide rVI (50 μM) alone, but not peptide I,control peptide or buffer, induced GVBD. Maturation initiated with alonger delay (about 6-7 hours) than in the control insulin-inducedoocytes in FIG. 5A (about 4-5 hours), and reached a plateau of about 50%GVBD.

Together, the data above indicate that peptides homologous to the WD-40region of RACK1 modulate the function of PKC. Peptide I inhibitedPKC-mediated oocyte maturation by about 40%, whereas peptide rVIpotentiated insulin-induced maturation, and resulted in a limitedmaturation response even in the absence of insulin. The latter resultsuggests that peptide rVI, under appropriate circumstances, may act toactivate PKC in the absence of other activating substances.

EXAMPLE 8 Effects of RACK1 WD-40-derived Peptides on PKC Translocationin Xenopus Oocytes

A. Buffers

Homogenization buffer: 20 mM Tris HCl, pH 7.5, 10 mM EGTA, 2 mM EDTA,0.25M sucrose, 10 μM phenylmethylsulfonyl fluoride, 20 μg/ml of eachleupeptin and soybean trypsin inhibitor.

B. PKC Translocation in Oocytes

Insulin causes the translocation of βPKC, but not other PKC isozymes,from a cytosolic form to a membrane-associated form, as evidenced by therelative levels of PKC in the soluble vs. the particulate fraction ofoocyte homogenate. To assess the effects of RACK1 WD-40-derived peptideson insulin-induced PKC translocation, 50 nl of a 20 mM NaCl solutioncontaining the indicated peptides were microinjected into Xenopusoocytes. The oocytes were then homogenized, and the relative amount ofPKC in the soluble and particulate fractions was assayed. The protocolfollowed was a modification of a method described by Smith, et al.(1992). The results are shown in FIG. 6.

Batches of 50 oocytes were microinjected with either peptide rVI (SEQ IDNO:7; 50 μM; lanes 3, 4), peptide I (SEQ ID NO:1; 50 μM, lanes 7, 8) orinjection solution (NaCl 20 mM, lanes 1,2 and 5,6). Homogenates fromeach batch were prepared 60 minutes after microinjection (lanes 1-4) or60 minutes after addition of insulin (lanes 5-8). The homogenates werecentrifuged at 10,000 g for 3 minutes, the upper layer (containing fatand yolk) was removed, and the remainder was frozen at −70° C. Prior touse, the samples were thawed, 200 μl homogenization buffer was added andthe samples were centrifuged at 100,000 g for 30 minutes at 4° C. Thesupernatants (soluble fraction) were removed and concentrated to 20 μlusing “CENTRICON” concentrators (Amicon, Beverly, Mass.). The pellets(particulate fractions) were dissolved in 20 μl of homogenizationbuffer. The samples were resolved on an 8% SDS/PAGE gel and blotted ontonitrocellulose. The amount of PKC in each fraction was determined byWestern blot using anti-βPKC antibodies (1:1000 dilution; SeikagakuKogyo, Tokyo, Japan). Bound primary antibodies were detected bychemiluminescence as described in Example 3, part C.

The antibodies showed immunoreactivity with an ˜80 kDa protein thatcorresponds to βPKC. Data are representative of three experiments.

The data are shown in FIG. 6. Lanes 1, 3, 5 and 7 contain particulatefractions (p), while lanes 2, 4, 6 and 8 contain soluble (cytosol)fractions (c). Peptide I (50 μM) did not affect βPKC distribution inuntreated oocytes, but inhibited insulin-induced βPKC translocation(FIG. 3, lanes 7,8). In contrast, peptide rVI (50 μM) induced βPKCtranslocation in the absence of insulin treatment (FIG. 3, lanes 3,4).

The results above suggest that peptide I is an antagonist ofinsulin-induced PKC translocation, whereas peptide rVI is an agonist andan activator of PKC translocation. In light of the results presented inExample 7, the data also suggest that the inhibition of insulin-inducedGVBD following microinjection of peptide I was due to an inhibition ofβPKC translocation.

EXAMPLE 9 Effects of RACK1 WD-40-derived Peptides on Sensitivity of PKCto Arg-C Endopeptidase

A. Buffers

Sample buffer: 0.3 M Tris HCl, 5% SDS, 50% glycerol, 0.01% bromophenolblue and 5% β-mercaptoethanol.

B. Nicking of βPKC by Arg-C Endopeptidase

Upon activation of PKC, a pseudosubstrate autoinhibitory sequence at theN-terminus of the molecule dissociates from the catalytic site andbecomes sensitive to endopeptidase Arg-C (Orr, et al.). In the absenceof PKC activators, exposure of the 80 kDa βPKC to endopeptidase Arg-Chas no effect on the enzyme (see FIG. 7, lane 1). In the presence of thePKC activators PS, DG and calcium, however, exposure of βPKC to Arg-Cresults in a “nicking” of the PKC (i.e. limited proteolysis generating a78 kDa fragment and several small fragments (see FIG. 7, lane 2)).Continued exposure to Arg-C results in the disappearance of βPKC (Orr,et al.). The present experiment tests whether peptides derived from theWD-40 region of RACK1 alter the sensitivity of βPKC to endopeptidaseArg-C.

The methods used to assay Arg-C sensitivity are a modification ofmethods described by Orr, et al. Rat brain PKC (˜5 nM) was incubated atroom temperature in 500 μl of 20 mM Tris-HCl buffer (pH 7.5) alone orwith Arg-C (5 units/ml) in the presence or absence of the indicatedpeptides (final concentration 10 μM or as indicated), PS, DG, andcalcium (as indicated). 50 μl aliquots were removed into 20 μl of samplebuffer during the reaction as indicated (samples in all the lanes wereincubated for 30 minutes, except lanes 5, and 6, which were incubatedfor 5 and 15 minutes, respectively). The samples were boiled for 10minutes at 80° C. and loaded onto 8% SDS-PAGE. βPKC was detected byWestern blot analysis using anti-βPKC antibodies as described inExamples 6 and 8.

The results are shown in FIG. 7. PKC was incubated for the indicatedtime alone (lane 1) or in the presence of Arg-C (lanes 2-9), with DG(0.8 μg/ml), PS (50 μg/ml) and CaCl₂ (1 mM; lane 2), with PS (50 μg/ml)and CaCl₂ (1 mM; lane 3), with PS (2.5 μg/ml) and CaCl₂ (50 μM; lane 4);with PS (2.5 μg/ml), CaCl₂ (50 μM) and with either peptide rVI (SEQ IDNO:7; 10 μM; lanes 5-7), control peptide (SEQ ID NO:9; lane 8) or withpeptide I (SEQ ID NO:1; lane 9).

Incubation of βPKC with Arg-C at low concentrations of activators (2.5μg/ml PS and 50 μM CaCl₂) in the absence of added peptide did not resultin appreciable nicking activity (FIG. 7, lane 4). Similarly, nicking ofβPKC did not occur in the presence of this concentration of activatorswith peptide I (lane 9) or with control peptide (lane 8). However,incubation of βPKC with the same concentration of activators in thepresence of peptide rVI resulted in a time-dependent appearance of the78 kDa nicked PKC fragment (FIG. 4, lanes 5-7). Concentrations as low as10 nM of peptide rVI were sufficient to result in nicking activity,indicative of βPKC activation. The results indicate that peptide rVI,but not peptide I, is effective to stabilize PKC in an activatedconformation that renders it susceptible to Arg-C under conditions oflow PKC activators that would otherwise not render the enzymesusceptible to Arg-C.

EXAMPLE 10 Effects of RACK1 WD-40-derived Peptides on PKCAutophosphorylation

Activated PKC is capable of autophosphorylation. Since peptide rVI (SEQID NO:7) was effective to induce PKC translocation and GVBD in theabsence of an activator such as insulin, the ability of the peptide toinduce PKC autophosphorylation in the absence of PKC activators wasassessed.

PKC autophosphorylation in the presence of βPKC pseudosubstrateantibodies or the indicated peptides was carried out using amodification of the method described by Makowske, et al.Anti-pseudosubstrate antibodies, which were shown previously to induceautophosphorylation in the absence of PKC activators (Makowske, et al.)were used as a positive control. The results are shown in FIG. 8.

Rat brain PKC (˜10 nM) was incubated with mild agitation in a finalvolume of 250 μl of overlay buffer, as in Example 1 either withanti-βPKC pseudosubstrate antibodies (1:10 dilution, Life Technologies,Gaithersburg, Md.) or with the indicated peptide (10 μM). Whereindicated, PS (50 μg/ml), DG (0.8 μg/ml) and CaCl₂ (1 mM) were alsoadded. The amount of autophosphorylation was determined after 2 hoursfor the reaction with the anti-pseudosubstrate antibodies, or after 15minutes for the other samples. 50 μl of a buffer comprised of 20 mMTris-HCl (pH 7.5), 20 mM MgCl₂, 20 μM ATP and 5 μci/ml [γ-³²P]ATP. Themixture was incubated for 15 minutes at room temperature and thereaction was stopped by adding 60 μl sample buffer (see Example 9). Thesamples were then boiled for 10 minutes, loaded onto a 10% SDS-PAGE minigel and electrophoresed. The gel was fixed with 50% methanol and 10%acetic acid for 1 hour, and the autophosphorylation of PKC wasdetermined by autoradiography.

The results in FIG. 8 show PKC autophosphorylation in the presence ofDG, PS, and calcium (lane 1), in the presence of EGTA (lane 2), in thepresence of anti-βPKC pseudosubstrate antibodies (diluted 1:10 in 20 mMTris-HCl; lane 3), in the presence of peptide rVI (SEQ ID NO:7; 10 μM;lane 4), in the presence of peptide I (SEQ ID NO:1; 10 μM; lane 5), orin the presence of control peptide (SEQ ID NO:9; 10 μM; lane 6).

Peptide rVI in the absence of PKC activators induced PKCautophosphorylation to over 80% of the autophosphorylation obtained inthe presence of optimal concentration of PS, DG, and calcium (compareFIG. 8 lane 1 (control) with lane 4 (peptide rVI). Neither peptide I norcontrol peptide induced PKC autophosphorylation in the absence of PKCactivators (FIG. 8 lanes 5 and 6, respectively).

EXAMPLE 11 Effects of RACK1 WD-40-derived Peptides on HistonePhosphorylation by PKC

Incubation of PKC with peptide rVI (SEQ ID NO:7) induced histonephosphorylation by PKC. The method used was a modification of theprotocol described by Mochly-Rosen, et al. (1987). The results are shownin FIG. 9.

Histone type IIIs (Sigma Chemical Company, St. Louis, Mo.) wasphosphorylated by PKC (˜10 nM) in the absence (lane 1) and presence ofpeptide rVI (10 μM) (lanes 2 and 3) and in the presence and absence ofDG (0.8 μg/ml), PS (50 μg/ml) and CaCl₂ (1 mM) (lane 3). The results areexpressed as percentage of control that is the amount of Histonephosphorylation by PKC in the presence of DG (0.8 μg/ml), PS (50 μg/ml)and CaCl₂ (1 mM). The results are the average ±SEM of two independentexperiments. PKC was first incubated with the peptide rVI (10 μM) for 15minutes in overlay buffer as described above. Histone type IIIs (40μg/ml) was added in Tris-HCl (20 mM), MgCl₂ (20 mM), ATP (20 μM) and[γ-³²P]ATP (5 μci/ml) with or without PS (50 μg/ml), DG (0.8 μg/ml) andCaCl₂ (1 mM). Histone phosphorylation was determined by autoradiographyas above.

PKC activators PS, DG, and calcium were not required for either peptiderVI-induced autophosphorylation or histone phosphorylation, suggestingthat peptide rVI is an agonist of PKC activation.

In a related experiment, phosphorylation of histone type IIIs (25 μM) byPKC (10 nM) was not inhibited by RACK1; rather, a 4.5±0.1 fold increaseof histone phosphorylation occurred when co-incubated with ˜100 nM RACK1(n=2).

SEQUENCE LISTING (1) GENERAL INFORMATION: (iii) NUMBER OF SEQUENCES: 265(2) INFORMATION FOR SEQ ID NO:1: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: Peptide I (xi) SEQUENCEDESCRIPTION: SEQ ID NO:1: Lys Gly Asp Tyr Glu Lys Ile Leu Val Ala LeuCys Gly Gly Asn 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide, rI, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Val Thr GlnIle Ala Thr Thr 1 5 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide rII, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3: Phe Val SerAsp Val Val Ile 1 5 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide rIII, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Asp ValLeu Ser Val Ala Phe 1 5 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:peptide rIV, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Val Ser CysVal Arg Phe Ser 1 5 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide rV, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6: Gly Tyr LeuAsn Thr Val Thr 1 5 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide rVI, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: Asp Ile IleAsn Ala Leu Cys Phe 1 5 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Peptide rVII, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Pro GlnCys Thr Ser Leu Ala 1 5 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 6 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:control peptide 1, homol. to RACK1 261-266, LKGKIL (xi) SEQUENCEDESCRIPTION: SEQ ID NO:9: Leu Lys Gly Lys Ile Leu 1 5 (2) INFORMATIONFOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: control peptide 2, iden. to RACK1, 265 to 270IIVDEL (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Ile Ile Val Asp Glu Leu1 5 (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: PKC substrate peptide, (Ser25)PKC(19-36) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: Arg Phe Ala Arg LysGly Ser Leu Arg Gln Lys Asn Val His Glu Val 1 5 10 15 Lys Asn (2)INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: PKC Pseudosubstrate Inhibitor(PCK(19-36)) (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12: Arg Phe Ala ArgLys Gly Ala Leu Arg Gln Lys Asn Val His Glu Val 1 5 10 15 Lys Asn (2)INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: GBH Peptide, rI, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:13: Trp Val Thr Gln Ile Ala Thr Thr Pro Gln PhePro Asp Met Ile 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GBHPeptide rII, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Phe ValSer Asp Val Val Ile Ser Ser Asp Gly Gln Phe Ala Leu 1 5 10 15 (2)INFORMATION FOR SEQ ID NO:15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: GBH Peptide rIII, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:15: Asp Val Leu Ser Val Ala Phe Ser Ser Asp AsnArg Gln Ile Val 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GBHPeptide rIV, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Trp ValSer Cys Val Arg Phe Ser Pro Asn Ser Ser Asn Pro Ile 1 5 10 15 (2)INFORMATION FOR SEQ ID NO:17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:15 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: GBH Peptide rV, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:17: Tyr Leu Asn Thr Val Thr Val Ser Pro Asp GlySer Leu Cys Ala 1 5 10 15 (2) INFORMATION FOR SEQ ID NO:18: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 15 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GBHPeptide rVI, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: Thr LeuAsp Gly Gly Asp Ile Ile Asn Ala Leu Cys Phe Ser Pro 1 5 10 15 (2)INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:1115 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D)TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL:NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:RACK1 DNA Sequence, Fig. 1A (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19:GGCACGAGGG GTCGCGGTGG CAGCCGTGCG GTGCTTGGCT CCCTAAGCTA TCCGGTGCCA 60TCCTTGTCGC TGCGGCGACT CGCAACATCT GCAGCCATGA CCGAGCAAAT GACCCTTCGT 120GGGACCCTCA AGGGCCATAA TGGATGGGTT ACACAGATCG CCACCACTCC GCAGTTCCCG 180GACATGATCC TGTCGGCGTC TCGAGACAAG ACCATCATCA TGTGGAAGCT GACCAGGGAT 240GAGACCAACT ACGGCATACC ACAACGTGCT CTTCGAGGTC ACTCCCACTT TGTTAGCGAT 300GTTGTCATCT CCTCTGATGG CCAGTTTGCC CTCTCAGGCT CCTGGGATGG AACCCTACGC 360CTCTGGGATC TCACAACGGG CACTACCACG AGACGATTTG TCGGCCACAC CAAGGATGTG 420CTGAGCGTGG CTTTCTCCTC TGACAACCGG CAGATTGTCT CTGGGTCCCG AGACAAGACC 480ATTAAGTTAT GGAATACTCT GGGTGTCTGC AAGTACACTG TCCAGGATGA GAGTCATTCA 540GAATGGGTGT CTTGTGTCCG CTTCTCCCCG AACAGCAGCA ACCCTATCAT CGTCTCCTGC 600GGATGGGACA AGCTGGTCAA GGTGTGGAAT CTGGCTAACT GCAAGCTAAA GACCAACCAC 660ATTGGCCACA CTGGCTATCT GAACACAGTG ACTGTCTCTC CAGATGGATC CCTCTGTGCT 720TCTGGAGGCA AGGATGGCCA GGCTATGCTG TGGGATCTCA ATGAAGGCAA GCACCTTTAC 780ACATTAGATG GTGGAGACAT CATCAATGCC TTGTGCTTCA GCCCCAACCG CTACTGGCTC 840TGTGCTGCCA CTGGCCCCAG TATCAAGATC TGGGACTTGG AGGGCAAGAT CATGGTAGAT 900GAACTGAAGC AAGAAGTTAT CAGCACCAGC AGCAAGGCAG AGCCACCCCA GTGTACCTCT 960TTGGCTTGGT CTGCTGATGG CCAGACTCTG TTTGCTGGCT ATACCGACAA CTTGGTGCGT 1020GTATGGCAGG TGACTATTGG TACCCGCTAA AAGTTTATGA CAGACTCTTA GAAATAAACT 1080GGCTTTCTGA AAAAAAAAAA AAAAAAAAAA AAAAA 1115 (2) INFORMATION FOR SEQ IDNO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 96 base pairs (B) TYPE:nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULETYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RACK1 rI DNA Sequence, Fig. 1A(xi) SEQUENCE DESCRIPTION: SEQ ID NO:20: GGCCATAATG GATGGGTTACACAGATCGCC ACCACTCCGC AGTTCCCGGA CATGATCCTG 60 TCGGCGTCTC GAGACAAGACCATCATCATG TGGAAG 96 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 94 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA(genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: RACK1 rII DNA Sequence (xi) SEQUENCEDESCRIPTION: SEQ ID NO:21: GGTCACTCCC ACTTTGTTAG CGATGTTGTC ATCTCCTCTGATGGCCAGTT TGCCCTCTCA 60 GGCTCCTGGG ATGGAACCCT ACGCCTCTGG GATC 94 (2)INFORMATION FOR SEQ ID NO:22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:93 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D)TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL:NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:RACK1 rIII DNA Sequence, Fig. 1A (xi) SEQUENCE DESCRIPTION: SEQ IDNO:22: GGCCACACCA AGGATGTGCT GAGCGTGGCT TTCTCCTCTG ACAACCGGCA GATTGTCTCT60 GGGTCCCGAG ACAAGACCAT TAAGTTATGG AAT 93 (2) INFORMATION FOR SEQ IDNO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 99 base pairs (B) TYPE:nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULETYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RACK1 rIV DNA Sequence, Fig. 1A(xi) SEQUENCE DESCRIPTION: SEQ ID NO:23: AGTCATTCAG AATGGGTGTCTTGTGTCCGC TTCTCCCCGA ACAGCAGCAA CCCTATCATC 60 GTCTCCTGCG GATGGGACAAGCTGGTCAAG GTGTGGAAT 99 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 93 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA(genomic) (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: RACK1 rV DNA Sequence, Fig. 1A (xi)SEQUENCE DESCRIPTION: SEQ ID NO:24: GGCCACACTG GCTATCTGAA CACAGTGACTGTCTCTCCAG ATGGATCCCT CTGTGCTTCT 60 GGAGGCAAGG ATGGCCAGGC TATGCTGTGG GAT93 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 93 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double(D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 rVI DNA Sequence, Fig. 1A (xi) SEQUENCEDESCRIPTION: SEQ ID NO:25: TTAGATGGTG GAGACATCAT CAATGCCTTG TGCTTCAGCCCCAACCGCTA CTGGCTCTGT 60 GCTGCCACTG GCCCCAGTAT CAAGATCTGG GAC 93 (2)INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:99 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D)TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL:NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:RACK1 rVII DNA Sequence, Fig. 1A (xi) SEQUENCE DESCRIPTION: SEQ IDNO:26: AGCAAGGCAG AGCCACCCCA GTGTACCTCT TTGGCTTGGT CTGCTGATGG CCAGACTCTG60 TTTGCTGGCT ATACCGACAA CTTGGTGCGT GTATGGCAG 99 (2) INFORMATION FOR SEQID NO:27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 317 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 Amino Acid Sequence, Fig. 1C (xi) SEQUENCEDESCRIPTION: SEQ ID NO:27: Met Thr Glu Gln Met Thr Leu Arg Gly Thr LeuLys Gly His Asn Gly 1 5 10 15 Trp Val Thr Gln Ile Ala Thr Thr Pro GlnPhe Pro Asp Met Ile Leu 20 25 30 Ser Ala Ser Arg Asp Lys Thr Ile Ile MetTrp Lys Leu Thr Arg Asp 35 40 45 Glu Thr Asn Tyr Gly Ile Pro Gln Arg AlaLeu Arg Gly His Ser His 50 55 60 Phe Val Ser Asp Val Val Ile Ser Ser AspGly Gln Phe Ala Leu Ser 65 70 75 80 Gly Ser Trp Asp Gly Thr Leu Arg LeuTrp Asp Leu Thr Thr Gly Thr 85 90 95 Thr Thr Arg Arg Phe Val Gly His ThrLys Asp Val Leu Ser Val Ala 100 105 110 Phe Ser Ser Asp Asn Arg Gln IleVal Ser Gly Ser Arg Asp Lys Thr 115 120 125 Ile Lys Leu Trp Asn Thr LeuGly Val Cys Lys Tyr Thr Val Gln Asp 130 135 140 Glu Ser His Ser Glu TrpVal Ser Cys Val Arg Phe Ser Pro Asn Ser 145 150 155 160 Ser Asn Pro IleIle Val Ser Cys Gly Trp Asp Lys Leu Val Lys Val 165 170 175 Trp Asn LeuAla Asn Cys Lys Leu Lys Thr Asn His Ile Gly His Thr 180 185 190 Gly TyrLeu Asn Thr Val Thr Val Ser Pro Asp Gly Ser Leu Cys Ala 195 200 205 SerGly Gly Lys Asp Gly Gln Ala Met Leu Trp Asp Leu Asn Glu Gly 210 215 220Lys His Leu Tyr Thr Leu Asp Gly Gly Asp Ile Ile Asn Ala Leu Cys 225 230235 240 Phe Ser Pro Asn Arg Tyr Trp Leu Cys Ala Ala Thr Gly Pro Ser Ile245 250 255 Lys Ile Trp Asp Leu Glu Gly Lys Ile Ile Val Asp Glu Leu LysGln 260 265 270 Glu Val Ile Ser Thr Ser Ser Lys Ala Glu Pro Pro Gln CysThr Ser 275 280 285 Leu Ala Trp Ser Ala Asp Gly Gln Thr Leu Phe Ala GlyTyr Thr Asp 290 295 300 Asn Leu Val Arg Val Trp Gln Val Thr Ile Gly ThrArg 305 310 315 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 501 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: Human55 kDa protein (PWP homolog), Fig. 11 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:28: Met Asn Arg Ser Arg Gln Val Thr Cys Val Ala Trp Val Arg Cys Gly 15 10 15 Val Ala Lys Glu Thr Pro Asp Lys Val Glu Leu Ser Lys Glu Glu Val20 25 30 Lys Arg Leu Ile Ala Glu Ala Lys Glu Lys Leu Gln Glu Glu Gly Gly35 40 45 Gly Ser Asp Glu Glu Glu Thr Gly Ser Pro Ser Glu Asp Gly Met Gln50 55 60 Ser Ala Arg Thr Gln Ala Arg Pro Arg Glu Pro Leu Glu Asp Gly Asp65 70 75 80 Pro Glu Asp Asp Arg Thr Leu Asp Asp Asp Glu Leu Ala Glu TyrAsp 85 90 95 Leu Asp Lys Tyr Asp Glu Glu Gly Asp Pro Asp Ala Glu Thr LeuGly 100 105 110 Glu Ser Leu Leu Gly Leu Thr Val Tyr Gly Ser Asn Asp GlnAsp Pro 115 120 125 Tyr Val Thr Leu Lys Asp Thr Glu Gln Tyr Glu Arg GluAsp Phe Leu 130 135 140 Ile Lys Pro Ser Asp Asn Leu Ile Val Cys Gly ArgAla Glu Gln Asp 145 150 155 160 Gln Cys Asn Leu Glu Val His Val Tyr AsnGln Glu Glu Asp Ser Phe 165 170 175 Tyr Val His His Asp Ile Leu Leu SerAla Tyr Pro Leu Ser Val Glu 180 185 190 Trp Leu Asn Phe Asp Pro Ser ProAsp Asp Ser Thr Gly Asn Tyr Ile 195 200 205 Ala Val Gly Asn Met Thr ProVal Ile Glu Val Trp Asp Leu Asp Ile 210 215 220 Val Asp Ser Leu Glu ProVal Phe Thr Leu Gly Ser Lys Leu Ser Lys 225 230 235 240 Lys Lys Lys LysLys Gly Lys Lys Ser Ser Ser Ala Glu Gly His Thr 245 250 255 Asp Ala ValLeu Asp Leu Ser Trp Asn Lys Leu Ile Arg Asn Val Leu 260 265 270 Ala SerAla Ser Ala Asp Asn Thr Val Ile Leu Trp Asp Met Ser Leu 275 280 285 GlyLys Pro Ala Ala Ser Leu Ala Val His Thr Asp Lys Val Gln Thr 290 295 300Leu Gln Phe His Pro Phe Glu Ala Gln Thr Leu Ile Ser Gly Ser Tyr 305 310315 320 Asp Lys Ser Val Ala Leu Tyr Asp Cys Arg Ser Pro Asp Glu Ser His325 330 335 Arg Met Trp Arg Phe Ser Gly Gln Ile Glu Arg Val Thr Trp AsnHis 340 345 350 Phe Ser Pro Cys His Phe Leu Ala Ser Thr Asp Asp Gly PheVal Tyr 355 360 365 Asn Leu Asp Ala Arg Ser Asp Lys Pro Ile Phe Thr LeuAsn Ala His 370 375 380 Asn Asp Glu Ile Ser Gly Leu Asp Leu Ser Ser GlnIle Lys Gly Cys 385 390 395 400 Leu Val Thr Ala Ser Ala Asp Lys Tyr ValLys Ile Trp Asp Ile Leu 405 410 415 Gly Asp Arg Pro Ser Leu Val His SerArg Asp Met Lys Met Gly Val 420 425 430 Leu Phe Cys Ser Ser Cys Cys ProAsp Leu Pro Phe Ile Tyr Ala Phe 435 440 445 Gly Gly Gln Lys Glu Gly LeuArg Val Trp Asp Ile Ser Thr Val Ser 450 455 460 Ser Val Asn Glu Ala PheGly Arg Arg Glu Arg Leu Val Leu Gly Ser 465 470 475 480 Ala Arg Asn SerSer Ile Ser Gly Pro Phe Gly Ser Arg Ser Ser Asp 485 490 495 Thr Pro MetGlu Ser 500 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 428 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:AAC-RICH protein, Fig. 12 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29: ProGly Gly Phe Gln His Leu Gln Gln Gln Gln Gln Gln Gln Gln Gln 1 5 10 15Gln Gln Gln Gln Gln Gln Gln Gln Gln Gln Gln Gln Thr Gln Val Gln 20 25 30Gln Leu His Asn Gln Leu His Gln Gln His Asn Gln Gln Ile Gln Gln 35 40 45Gln Ala Gln Ala Thr Gln Gln His Leu Gln Thr Gln Gln Tyr Leu Gln 50 55 60Ser Gln Ile His Gln Gln Ser Gln Gln Ser Gln Leu Ser Asn Asn Leu 65 70 7580 Asn Ser Asn Ser Lys Glu Ser Thr Asn Ile Pro Lys Thr Asn Thr Gln 85 9095 Tyr Thr Asn Phe Asp Ser Lys Asn Leu Asp Leu Ala Ser Arg Tyr Phe 100105 110 Ser Glu Cys Ser Thr Lys Asp Phe Ile Gly Asn Lys Lys Lys Ser Thr115 120 125 Ser Val Ala Trp Asn Ala Asn Gly Thr Lys Ile Ala Ser Ser GlySer 130 135 140 Asp Gly Ile Val Arg Val Trp Asn Phe Asp Pro Leu Gly AsnSer Asn 145 150 155 160 Asn Asn Asn Asn Ser Asn Asn Thr Ser Ser Asn SerLys Asn Asn Asn 165 170 175 Ile Lys Glu Thr Ile Glu Leu Lys Gly His AspGly Ser Ile Glu Lys 180 185 190 Ile Ser Trp Ser Pro Lys Asn Asn Asp LeuLeu Ala Ser Ala Gly Thr 195 200 205 Asp Lys Val Ile Lys Ile Trp Asp ValLys Ile Gly Lys Cys Ile Gly 210 215 220 Thr Val Ser Thr Asn Ser Glu AsnIle Asp Val Arg Trp Ser Pro Asp 225 230 235 240 Gly Asp His Leu Ala LeuIle Asp Leu Pro Thr Ile Lys Thr Leu Lys 245 250 255 Ile Tyr Lys Phe AsnGly Glu Glu Leu Asn Gln Val Gly Trp Asp Asn 260 265 270 Asn Gly Asp LeuIle Leu Met Ala Asn Ser Met Gly Asn Ile Glu Ala 275 280 285 Tyr Lys PheLeu Pro Lys Ser Thr Thr His Val Lys His Leu Lys Thr 290 295 300 Leu TyrGly His Thr Ala Ser Ile Tyr Cys Met Glu Phe Asp Pro Thr 305 310 315 320Gly Lys Tyr Leu Ala Ala Gly Ser Ala Asp Ser Ile Val Ser Leu Trp 325 330335 Asp Ile Glu Asp Met Met Cys Val Lys Thr Phe Ile Lys Ser Thr Phe 340345 350 Pro Cys Arg Ser Val Ser Phe Ser Phe Asp Gly Gln Phe Ile Ala Ala355 360 365 Ser Ser Phe Glu Ser Thr Ile Glu Ile Phe His Ile Glu Ser SerGln 370 375 380 Pro Ile His Thr Ile Glu Cys Gly Val Ser Ser Leu Met TrpHis Pro 385 390 395 400 Thr Leu Pro Leu Leu Ala Tyr Ala Pro Glu Ser IleAsn Glu Asn Asn 405 410 415 Lys Asp Pro Ser Ile Arg Val Phe Gly Tyr HisSer 420 425 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 517 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: BETATRCP, Fig. 13 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30: Met Glu Gly PheSer Cys Ser Leu Gln Pro Pro Thr Ala Ser Glu Arg 1 5 10 15 Glu Asp CysAsn Arg Asp Glu Pro Pro Arg Lys Ile Ile Thr Glu Lys 20 25 30 Asn Thr LeuArg Gln Thr Lys Leu Ala Asn Gly Thr Ser Ser Met Ile 35 40 45 Val Pro LysGln Arg Lys Leu Ser Ala Asn Tyr Glu Lys Glu Lys Glu 50 55 60 Leu Cys ValLys Tyr Phe Glu Gln Trp Ser Glu Cys Asp Gln Val Glu 65 70 75 80 Phe ValGlu His Leu Ile Ser Arg Met Cys His Tyr Gln His Gly His 85 90 95 Ile AsnThr Tyr Leu Lys Pro Met Leu Gln Arg Asp Phe Ile Thr Ala 100 105 110 LeuPro Ala Arg Gly Leu Asp His Ile Ala Glu Asn Ile Leu Ser Tyr 115 120 125Leu Asp Ala Lys Ser Leu Cys Ser Ala Glu Leu Val Cys Lys Glu Trp 130 135140 Tyr Arg Val Thr Ser Asp Gly Met Leu Trp Lys Lys Leu Ile Glu Arg 145150 155 160 Met Val Arg Thr Asp Ser Leu Trp Arg Gly Leu Ala Glu Arg ArgGly 165 170 175 Trp Gly Gln Tyr Leu Phe Lys Asn Lys Pro Pro Asp Gly LysThr Pro 180 185 190 Pro Asn Ser Phe Tyr Arg Ala Leu Tyr Pro Lys Ile IleGln Asp Ile 195 200 205 Glu Thr Ile Glu Ser Asn Trp Arg Cys Gly Arg HisSer Leu Gln Arg 210 215 220 Ile His Cys Arg Ser Glu Thr Ser Lys Gly ValTyr Cys Leu Gln Tyr 225 230 235 240 Asp Asp Gln Lys Ile Val Ser Gly LeuArg Asp Asn Thr Ile Lys Ile 245 250 255 Trp Asp Lys Asn Thr Leu Glu CysLys Arg Val Leu Met Gly His Thr 260 265 270 Gly Ser Val Leu Cys Leu GlnTyr Asp Glu Arg Val Ile Ile Thr Gly 275 280 285 Ser Asp Ser Thr Val ArgVal Trp Asp Val Asn Thr Gly Glu Met Leu 290 295 300 Asn Thr Leu Ile HisHis Cys Glu Ala Val Leu His Leu Arg Phe Asn 305 310 315 320 Asn Gly MetMet Val Thr Cys Ser Lys Asp Arg Ser Ile Ala Val Trp 325 330 335 Asp MetAla Ser Ala Thr Asp Ile Thr Leu Arg Arg Val Leu Val Gly 340 345 350 HisArg Ala Ala Val Asn Val Val Asp Phe Asp Asp Lys Tyr Ile Val 355 360 365Ser Ala Ser Gly Asp Arg Thr Ile Lys Val Trp Asn Thr Ser Thr Cys 370 375380 Glu Phe Val Arg Thr Leu Asn Gly His Lys Arg Gly Ile Ala Cys Leu 385390 395 400 Gln Tyr Arg Asp Arg Leu Val Val Ser Gly Ser Ser Asp Asn ThrIle 405 410 415 Arg Leu Trp Asp Ile Glu Cys Gly Ala Cys Leu Arg Val LeuGlu Gly 420 425 430 His Glu Glu Leu Val Arg Cys Ile Arg Phe Asp Asn LysArg Ile Val 435 440 445 Ser Gly Ala Tyr Asp Gly Lys Ile Lys Val Trp AspLeu Val Ala Ala 450 455 460 Leu Asp Pro Arg Ala Pro Ala Gly Thr Leu CysLeu Arg Thr Leu Val 465 470 475 480 Glu His Ser Gly Arg Val Phe Arg LeuGln Phe Asp Glu Phe Gln Ile 485 490 495 Val Ser Ser Ser His Asp Asp ThrIle Leu Ile Trp Asp Phe Leu Asn 500 505 510 Asp Pro Gly Leu Ala 515 (2)INFORMATION FOR SEQ ID NO:31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:906 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: beta-prime-cop, Fig. 14 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:31: Met Pro Leu Arg Leu Asp Ile Lys Arg Lys LeuThr Ala Arg Ser Asp 1 5 10 15 Arg Val Lys Ser Val Asp Leu His Pro ThrGlu Pro Trp Met Leu Ala 20 25 30 Ser Leu Tyr Asn Gly Ser Val Cys Val TrpAsn His Glu Thr Gln Thr 35 40 45 Leu Val Lys Thr Phe Glu Val Cys Asp LeuPro Val Arg Ala Ala Lys 50 55 60 Phe Val Ala Arg Lys Asn Trp Val Val ThrGly Ala Asp Asp Met Gln 65 70 75 80 Ile Arg Val Phe Asn Tyr Asn Thr LeuGlu Arg Val His Met Phe Glu 85 90 95 Ala His Ser Asp Tyr Ile Arg Cys IleAla Val His Pro Thr Gln Pro 100 105 110 Phe Ile Leu Thr Ser Ser Asp AspMet Leu Ile Lys Leu Trp Asp Trp 115 120 125 Asp Lys Lys Trp Ser Cys SerGln Val Phe Glu Gly His Thr His Tyr 130 135 140 Val Met Gln Ile Val IleAsn Pro Lys Asp Asn Asn Gln Phe Ala Ser 145 150 155 160 Ala Ser Leu AspArg Thr Ile Lys Val Trp Gln Leu Gly Ser Ser Ser 165 170 175 Pro Asn PheThr Leu Glu Gly His Glu Lys Gly Val Asn Cys Ile Asp 180 185 190 Tyr TyrSer Gly Gly Asp Lys Pro Tyr Leu Ile Ser Gly Ala Asp Asp 195 200 205 ArgLeu Val Lys Ile Trp Asp Tyr Gln Asn Lys Thr Cys Val Gln Thr 210 215 220Leu Glu Gly His Ala Gln Asn Val Ser Cys Ala Ser Phe His Pro Glu 225 230235 240 Leu Pro Ile Ile Ile Thr Gly Ser Glu Asp Gly Thr Val Arg Ile Trp245 250 255 His Ser Ser Thr Tyr Arg Leu Glu Ser Thr Leu Asn Tyr Gly MetGlu 260 265 270 Arg Val Trp Cys Val Ala Ser Leu Arg Gly Ser Asn Asn ValAla Leu 275 280 285 Gly Tyr Asp Glu Gly Ser Ile Ile Val Lys Leu Gly ArgGlu Glu Pro 290 295 300 Ala Met Ser Met Asp Ala Asn Gly Lys Ile Ile TrpAla Lys His Ser 305 310 315 320 Glu Val Gln Gln Ala Asn Leu Lys Ala MetGly Asp Ala Glu Ile Lys 325 330 335 Asp Gly Glu Arg Leu Pro Leu Ala ValLys Asp Met Gly Ser Cys Glu 340 345 350 Ile Tyr Pro Gln Thr Ile Gln HisAsn Pro Asn Gly Arg Phe Val Val 355 360 365 Val Cys Gly Asp Gly Glu TyrIle Ile Tyr Thr Ala Met Ala Leu Arg 370 375 380 Asn Lys Ser Phe Gly SerAla Gln Glu Phe Ala Trp Ala His Asp Ser 385 390 395 400 Ser Glu Tyr AlaIle Arg Glu Ser Asn Ser Val Val Lys Ile Phe Lys 405 410 415 Asn Phe LysGlu Lys Lys Ser Phe Lys Pro Asp Phe Gly Ala Glu Ser 420 425 430 Ile TyrGly Gly Phe Leu Leu Gly Val Arg Ser Val Asn Gly Leu Ala 435 440 445 PheTyr Asp Trp Glu Asn Thr Glu Leu Ile Arg Arg Ile Glu Ile Gln 450 455 460Pro Lys His Ile Phe Trp Ser Asp Ser Gly Glu Leu Val Cys Ile Ala 465 470475 480 Thr Glu Glu Ser Phe Phe Ile Leu Lys Tyr Leu Ser Glu Lys Val Leu485 490 495 Ala Ala Gln Glu Thr His Glu Gly Val Thr Glu Asp Gly Ile GluAsp 500 505 510 Gly Phe Glu Val Leu Gly Glu Ile Gln Glu Ile Val Lys ThrGly Leu 515 520 525 Trp Val Gly Asp Cys Phe Ile Tyr Thr Ser Ser Val AsnArg Leu Asn 530 535 540 Tyr Tyr Val Gly Gly Glu Ile Val Thr Ile Ala HisLeu Asp Arg Thr 545 550 555 560 Met Tyr Leu Leu Gly Tyr Ile Pro Lys AspAsn Arg Leu Tyr Leu Gly 565 570 575 Asp Lys Glu Leu Asn Ile Val Ser TyrSer Leu Leu Val Ser Val Leu 580 585 590 Glu Tyr Gln Thr Ala Val Met ArgArg Asp Phe Ser Met Ala Asp Lys 595 600 605 Val Leu Pro Thr Ile Pro LysGlu Gln Arg Thr Arg Val Ala His Phe 610 615 620 Leu Glu Lys Gln Gly PheLys Gln Gln Ala Leu Thr Val Ser Thr Asp 625 630 635 640 Pro Glu His ArgPhe Glu Leu Ala Leu Gln Leu Gly Glu Leu Lys Ile 645 650 655 Ala Tyr GlnLeu Ala Val Glu Ala Glu Ser Glu Gln Lys Trp Lys Gln 660 665 670 Leu AlaGlu Leu Ala Ile Ser Lys Cys Pro Phe Gly Leu Ala Gln Glu 675 680 685 CysLeu His His Ala Gln Asp Tyr Gly Gly Leu Leu Leu Leu Ala Thr 690 695 700Ala Ser Gly Asn Ala Ser Met Val Asn Lys Leu Ala Glu Gly Ala Glu 705 710715 720 Arg Asp Gly Lys Asn Asn Val Ala Phe Met Ser Tyr Phe Leu Gln Gly725 730 735 Lys Leu Asp Ala Cys Leu Glu Leu Leu Ile Arg Thr Gly Arg LeuPro 740 745 750 Glu Ala Ala Phe Leu Ala Arg Thr Tyr Leu Pro Ser Gln ValSer Arg 755 760 765 Val Val Lys Leu Trp Arg Glu Asn Leu Ser Lys Val AsnGln Lys Ala 770 775 780 Ala Glu Ser Leu Ala Asp Pro Thr Glu Tyr Glu AsnLeu Phe Pro Gly 785 790 795 800 Leu Lys Glu Ala Phe Val Val Glu Glu TrpVal Lys Glu Thr His Ala 805 810 815 Asp Leu Trp Pro Ala Lys Gln Tyr ProLeu Val Thr Pro Asn Glu Glu 820 825 830 Arg Asn Val Met Glu Glu Ala LysGly Phe Gln Pro Ser Arg Ser Ala 835 840 845 Ala Gln Gln Glu Leu Asp GlyLys Pro Ala Ser Pro Thr Pro Val Ile 850 855 860 Val Thr Ser Gln Thr AlaAsn Lys Glu Glu Lys Ser Leu Leu Glu Leu 865 870 875 880 Glu Val Asp LeuAsp Asn Leu Glu Ile Glu Asp Ile Asp Thr Thr Asp 885 890 895 Ile Asn LeuAsp Glu Asp Ile Leu Asp Asp 900 905 (2) INFORMATION FOR SEQ ID NO:32:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 779 amino acids (B) TYPE:amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CDC4 / CDC20 protein, Fig. 15 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:32: Met Gly Ser Phe Pro Leu Ala Glu Phe Pro LeuArg Asp Ile Pro Val 1 5 10 15 Pro Tyr Ser Tyr Arg Val Ser Gly Gly IleAla Ser Ser Gly Ser Val 20 25 30 Thr Ala Leu Val Thr Ala Ala Gly Thr HisArg Asn Ser Ser Thr Ala 35 40 45 Lys Thr Val Glu Thr Glu Asp Gly Glu GluAsp Ile Asp Glu Tyr Gln 50 55 60 Arg Lys Arg Ala Ala Gly Ser Gly Glu SerThr Pro Glu Arg Ser Asp 65 70 75 80 Phe Lys Arg Val Lys His Asp Asn HisLys Thr Leu His Pro Val Asn 85 90 95 Leu Gln Asn Thr Gly Ala Ala Ser ValAsp Asn Asp Gly Leu His Asn 100 105 110 Leu Thr Asp Ile Ser Asn Asp AlaGlu Lys Leu Leu Met Ser Val Asp 115 120 125 Asp Gly Ser Ala Ala Pro SerThr Leu Ser Val Asn Met Gly Val Ala 130 135 140 Ser His Asn Val Ala AlaPro Thr Thr Val Asn Ala Ala Thr Ile Thr 145 150 155 160 Gly Ser Asp ValSer Asn Asn Val Asn Ser Ala Thr Ile Asn Asn Pro 165 170 175 Met Glu GluGly Ala Leu Pro Leu Ser Pro Thr Ala Ser Ser Pro Gly 180 185 190 Thr ThrThr Pro Leu Ala Lys Thr Thr Lys Thr Ile Asn Asn Asn Asn 195 200 205 AsnIle Ala Asp Leu Ile Glu Ser Lys Asp Ser Ile Ile Ser Pro Glu 210 215 220Tyr Leu Ser Asp Glu Ile Phe Ser Ala Ile Asn Asn Asn Leu Pro His 225 230235 240 Ala Tyr Phe Lys Asn Leu Leu Phe Arg Leu Val Ala Asn Met Asp Arg245 250 255 Ser Glu Leu Ser Asp Leu Gly Thr Leu Ile Lys Asp Asn Leu LysArg 260 265 270 Asp Leu Ile Thr Ser Leu Pro Phe Glu Ile Ser Leu Lys IlePhe Asn 275 280 285 Tyr Leu Gln Phe Glu Asp Ile Ile Asn Ser Leu Gly ValSer Gln Asn 290 295 300 Trp Asn Lys Ile Ile Arg Lys Ser Thr Ser Leu TrpLys Lys Leu Leu 305 310 315 320 Ile Ser Glu Asn Phe Val Ser Pro Lys GlyPhe Asn Ser Leu Asn Leu 325 330 335 Lys Leu Ser Gln Lys Tyr Pro Lys LeuSer Gln Gln Asp Arg Leu Arg 340 345 350 Leu Ser Phe Leu Glu Asn Ile PheIle Leu Lys Asn Trp Tyr Asn Pro 355 360 365 Lys Phe Val Pro Gln Arg ThrThr Leu Arg Gly His Met Thr Ser Val 370 375 380 Ile Thr Cys Leu Gln PheGlu Asp Asn Tyr Val Ile Thr Gly Ala Asp 385 390 395 400 Asp Lys Met IleArg Val Tyr Asp Ser Ile Asn Lys Lys Phe Leu Leu 405 410 415 Gln Leu SerGly His Asp Gly Gly Val Trp Ala Leu Lys Tyr Ala His 420 425 430 Gly GlyIle Leu Val Ser Gly Ser Thr Asp Arg Thr Val Arg Val Trp 435 440 445 AspIle Lys Lys Gly Cys Cys Thr His Val Phe Glu Gly His Asn Ser 450 455 460Thr Val Arg Cys Leu Asp Ile Val Glu Tyr Lys Asn Ile Lys Tyr Ile 465 470475 480 Val Thr Gly Ser Arg Asp Asn Thr Leu His Val Trp Lys Leu Pro Lys485 490 495 Glu Ser Ser Val Pro Asp His Gly Glu Glu His Asp Tyr Pro LeuVal 500 505 510 Phe His Thr Pro Glu Glu Asn Pro Tyr Phe Val Gly Val LeuArg Gly 515 520 525 His Met Ala Ser Val Arg Thr Val Ser Gly His Gly AsnIle Val Val 530 535 540 Ser Gly Ser Tyr Asp Asn Thr Leu Ile Val Trp AspVal Ala Gln Met 545 550 555 560 Lys Cys Leu Tyr Ile Leu Ser Gly His ThrAsp Arg Ile Tyr Ser Thr 565 570 575 Ile Tyr Asp His Glu Arg Lys Arg CysIle Ser Ala Ser Met Asp Thr 580 585 590 Thr Ile Arg Ile Trp Asp Leu GluAsn Ile Trp Asn Asn Gly Glu Cys 595 600 605 Ser Tyr Ala Thr Asn Ser AlaSer Pro Cys Ala Lys Ile Leu Gly Ala 610 615 620 Met Tyr Thr Leu Gln GlyHis Thr Ala Leu Val Gly Leu Leu Arg Leu 625 630 635 640 Ser Asp Lys PheLeu Val Ser Ala Ala Ala Asp Gly Ser Ile Arg Gly 645 650 655 Trp Asp AlaAsn Asp Tyr Ser Arg Lys Phe Ser Tyr His His Thr Asn 660 665 670 Leu SerAla Ile Thr Thr Phe Tyr Val Ser Asp Asn Ile Leu Val Ser 675 680 685 GlySer Glu Asn Gln Phe Asn Ile Tyr Asn Leu Arg Ser Gly Lys Leu 690 695 700Val His Ala Asn Ile Leu Lys Asp Ala Asp Gln Ile Trp Ser Val Asn 705 710715 720 Phe Lys Gly Lys Thr Leu Val Ala Ala Val Glu Lys Asp Gly Gln Ser725 730 735 Phe Leu Glu Ile Leu Asp Phe Ser Lys Ala Ser Lys Ile Asn TyrVal 740 745 750 Ser Asn Pro Val Asn Ser Ser Ser Ser Ser Leu Glu Ser IleSer Thr 755 760 765 Ser Leu Gly Leu Thr Arg Thr Thr Ile Ile Pro 770 775(2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 318 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG,Fig. 16 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33: Met Ala Glu Thr Leu ThrLeu Arg Ala Thr Leu Lys Gly His Thr Asn 1 5 10 15 Trp Val Thr Ala IleAla Thr Pro Leu Asp Pro Ser Ser Asn Thr Leu 20 25 30 Leu Ser Ala Ser ArgAsp Lys Ser Val Leu Val Trp Glu Leu Glu Arg 35 40 45 Ser Glu Ser Asn TyrGly Tyr Ala Arg Lys Ala Leu Arg Gly His Ser 50 55 60 His Phe Val Gln AspVal Val Ile Ser Ser Asp Gly Gln Phe Cys Leu 65 70 75 80 Thr Gly Ser TrpAsp Gly Thr Leu Arg Leu Trp Asp Leu Asn Thr Gly 85 90 95 Thr Thr Thr ArgArg Phe Val Gly His Thr Lys Asp Val Leu Ser Val 100 105 110 Ala Phe SerVal Asp Asn Arg Gln Ile Val Ser Gly Ser Arg Asp Lys 115 120 125 Thr IleLys Leu Trp Asn Thr Leu Gly Glu Cys Lys Tyr Thr Ile Gly 130 135 140 GluPro Glu Gly His Thr Glu Trp Val Ser Cys Val Arg Phe Ser Pro 145 150 155160 Met Thr Thr Asn Pro Ile Ile Val Ser Gly Gly Trp Asp Lys Met Val 165170 175 Lys Val Trp Asn Leu Thr Asn Cys Lys Leu Lys Asn Asn Leu Val Gly180 185 190 His His Gly Tyr Val Asn Thr Val Thr Val Ser Pro Asp Gly SerLeu 195 200 205 Cys Ala Ser Gly Gly Lys Asp Gly Ile Ala Met Leu Trp AspLeu Ala 210 215 220 Glu Gly Lys Arg Leu Tyr Ser Leu Asp Ala Gly Asp ValIle His Cys 225 230 235 240 Leu Cys Phe Ser Pro Asn Arg Tyr Trp Leu CysAla Ala Thr Gln Ser 245 250 255 Ser Ile Lys Ile Trp Asp Leu Glu Ser LysSer Ile Val Asp Asp Leu 260 265 270 Arg Pro Glu Phe Asn Ile Thr Ser LysLys Ala Gln Val Pro Tyr Cys 275 280 285 Val Ser Leu Ala Trp Ser Ala AspGly Ser Thr Leu Tyr Ser Gly Tyr 290 295 300 Thr Asp Gly Gln Ile Arg ValTrp Ala Val Gly His Ser Leu 305 310 315 (2) INFORMATION FOR SEQ IDNO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 658 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: cop-1 protein, Fig. 17 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:34: Met Glu Glu Ile Ser Thr Asp Pro Val Val Pro Ala Val LysPro Asp 1 5 10 15 Pro Arg Thr Ser Ser Val Gly Glu Gly Ala Asn Arg HisGlu Asn Asp 20 25 30 Asp Gly Gly Ser Gly Gly Ser Glu Ile Gly Ala Pro AspLeu Asp Lys 35 40 45 Asp Leu Leu Cys Pro Ile Cys Met Gln Ile Ile Lys AspAla Phe Leu 50 55 60 Thr Ala Cys Gly His Ser Phe Cys Tyr Met Cys Ile IleThr His Leu 65 70 75 80 Arg Asn Lys Ser Asp Cys Pro Cys Cys Ser Gln HisLeu Thr Asn Asn 85 90 95 Gln Leu Tyr Pro Asn Phe Leu Leu Asp Lys Leu LeuLys Lys Thr Ser 100 105 110 Ala Arg His Val Ser Lys Thr Ala Ser Pro LeuAsp Gln Phe Arg Glu 115 120 125 Ala Leu Gln Arg Gly Cys Asp Val Ser IleLys Glu Val Asp Asn Leu 130 135 140 Leu Thr Leu Leu Ala Glu Arg Lys ArgLys Met Glu Gln Glu Glu Ala 145 150 155 160 Glu Arg Asn Met Gln Ile LeuLeu Asp Phe Leu His Cys Leu Arg Lys 165 170 175 Gln Lys Val Asp Glu LeuAsn Glu Val Gln Thr Asp Leu Gln Tyr Ile 180 185 190 Lys Glu Asp Ile AsnAla Val Glu Arg His Arg Ile Asp Leu Tyr Arg 195 200 205 Ala Arg Asp ArgTyr Ser Val Lys Leu Arg Met Leu Gly Asp Asp Pro 210 215 220 Ser Thr ArgAsn Ala Trp Pro His Glu Lys Asn Gln Ile Gly Phe Asn 225 230 235 240 SerAsn Ser Leu Ser Ile Arg Gly Gly Asn Phe Val Gly Asn Tyr Gln 245 250 255Asn Lys Lys Val Glu Gly Lys Ala Gln Gly Ser Ser His Gly Leu Pro 260 265270 Lys Lys Asp Ala Leu Ser Gly Ser Asp Ser Gln Ser Leu Asn Gln Ser 275280 285 Thr Val Ser Met Ala Arg Lys Lys Arg Ile His Ala Gln Phe Asn Asp290 295 300 Leu Gln Glu Cys Tyr Leu Gln Lys Arg Arg Gln Leu Ala Asp GlnPro 305 310 315 320 Asn Ser Lys Gln Glu Asn Asp Lys Ser Val Val Arg ArgGlu Gly Tyr 325 330 335 Ser Asn Gly Leu Ala Asp Phe Gln Ser Val Leu ThrThr Phe Thr Arg 340 345 350 Tyr Ser Arg Leu Arg Val Ile Ala Glu Ile ArgHis Gly Asp Ile Phe 355 360 365 His Ser Ala Asn Ile Val Ser Ser Ile GluPhe Asp Arg Asp Asp Glu 370 375 380 Leu Phe Ala Thr Ala Gly Val Ser ArgCys Ile Lys Val Phe Asp Phe 385 390 395 400 Ser Ser Val Val Asn Glu ProAla Asp Met Gln Cys Pro Ile Val Glu 405 410 415 Met Ser Thr Arg Ser LysLeu Ser Cys Leu Ser Trp Asn Lys His Glu 420 425 430 Lys Asn His Ile AlaSer Ser Asp Tyr Glu Gly Ile Val Thr Val Trp 435 440 445 Asp Val Thr ThrArg Gln Ser Leu Met Glu Thr Glu Glu Asn Glu Lys 450 455 460 Arg Ala TrpSer Val Asp Phe Ser Arg Thr Glu Pro Ser Met Leu Val 465 470 475 480 SerGly Ser Asp Asp Cys Lys Val Lys Val Trp Cys Thr Arg Gln Glu 485 490 495Ala Ser Val Ile Asn Ile Asp Met Lys Ala Asn Ile Cys Cys Val Lys 500 505510 Tyr Asn Pro Gly Ser Ser Asn Tyr Ile Ala Val Gly Ser Ala Asp His 515520 525 His Ile His Tyr Tyr Asp Leu Arg Asn Ile Ser Gln Pro Leu His Val530 535 540 Phe Ser Gly His Lys Lys Ala Val Ser Tyr Met Lys Phe Leu SerAsn 545 550 555 560 Asn Glu Leu Ala Ser Ala Ser Thr Asp Ser Thr Leu ArgLeu Trp Asp 565 570 575 Val Lys Asp Asn Leu Pro Val Arg Thr Phe Arg GlyHis Thr Asn Glu 580 585 590 Lys Asn Phe Val Gly Leu Thr Val Asn Ser GluTyr Leu Ala Cys Gly 595 600 605 Ser Glu Thr Thr Arg Tyr Val Tyr His LysGlu Ile Thr Arg Pro Val 610 615 620 Thr Ser His Arg Phe Gly Ser Pro AspMet Asp Asp Ala Glu Lys Arg 625 630 635 640 Gln Val Pro Thr Leu Leu ValArg Phe Ala Gly Arg Val Ile Val Pro 645 650 655 Arg Cys (2) INFORMATIONFOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 440 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: CORO PROTEIN, Fig. 18 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:35: Met Ser Lys Val Val Arg Ser Ser Lys Tyr Arg His Val PheAla Ala 1 5 10 15 Gln Pro Lys Lys Glu Glu Cys Tyr Gln Asn Leu Lys ThrLys Ser Ala 20 25 30 Val Trp Asp Ser Asn Tyr Val Ala Ala Asn Thr Arg TyrIle Trp Asp 35 40 45 Ala Ala Gly Gly Gly Ser Phe Ala Val Glu Ala Ile ProHis Ser Gly 50 55 60 Lys Thr Thr Ser Val Pro Leu Phe Asn Gly His Lys SerAla Val Leu 65 70 75 80 Asp Ile Ala Phe His Pro Phe Asn Glu Asn Leu ValGly Ser Val Ser 85 90 95 Glu Asp Cys Asn Ile Cys Ile Trp Gly Ile Pro GluGly Gly Leu Thr 100 105 110 Asp Ser Ile Ser Thr Pro Leu Gln Thr Leu SerGly His Lys Arg Lys 115 120 125 Val Gly Thr Ile Ser Phe Gly Pro Val AlaAsp Asn Val Ala Val Thr 130 135 140 Ser Ser Gly Asp Phe Leu Val Lys ThrTrp Asp Val Glu Gln Gly Lys 145 150 155 160 Asn Leu Thr Thr Val Glu GlyHis Ser Asp Met Ile Thr Ser Cys Glu 165 170 175 His Asn Gly Ser Gln IleVal Thr Thr Cys Lys Asp Lys Lys Ala Arg 180 185 190 Val Phe Asp Pro ArgThr Asn Ser Ile Val Asn Glu Val Val Cys His 195 200 205 Gln Gly Val LysAsn Ser Arg Ala Ile Phe Ala Lys Asp Lys Val Ile 210 215 220 Thr Val GlyPhe Ser Lys Thr Ser Glu Arg Glu Leu His Ile Tyr Asp 225 230 235 240 ProArg Ala Phe Thr Thr Pro Leu Ser Ala Gln Val Val Asp Ser Ala 245 250 255Ser Gly Leu Leu Met Pro Phe Tyr Asp Ala Asp Asn Ser Ile Leu Tyr 260 265270 Leu Ala Gly Lys Gly Asp Gly Asn Ile Arg Tyr Tyr Glu Leu Val Asp 275280 285 Glu Ser Pro Tyr Ile His Phe Leu Ser Glu Phe Lys Ser Ala Thr Pro290 295 300 Gln Arg Gly Leu Cys Phe Leu Pro Lys Arg Cys Leu Asn Thr SerGlu 305 310 315 320 Cys Glu Ile Ala Arg Gly Leu Lys Val Thr Pro Phe ThrVal Glu Pro 325 330 335 Ile Ser Phe Arg Val Pro Arg Lys Ser Asp Ile PheGln Gly Asp Ile 340 345 350 Tyr Pro Asp Thr Tyr Ala Gly Glu Pro Ser LeuThr Ala Glu Gln Trp 355 360 365 Val Ser Gly Thr Asn Ala Glu Pro Lys ThrVal Ser Leu Ala Gly Gly 370 375 380 Phe Val Lys Lys Ala Ser Ala Val GluPhe Lys Pro Val Val Gln Val 385 390 395 400 Gln Glu Gly Pro Lys Asn GluLys Glu Leu Arg Glu Glu Tyr Glu Lys 405 410 415 Leu Lys Ile Arg Val AlaTyr Leu Glu Ser Glu Ile Val Lys Lys Asp 420 425 430 Ala Lys Ile Lys GluLeu Thr Asn 435 440 (2) INFORMATION FOR SEQ ID NO:36: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 445 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Coronin (p55), Fig. 19 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Met SerLys Val Val Arg Ser Ser Lys Tyr Arg His Val Phe Ala Ala 1 5 10 15 GlnPro Lys Lys Glu Glu Cys Tyr Gln Asn Leu Lys Val Thr Lys Ser 20 25 30 AlaTrp Asp Ser Asn Tyr Val Ala Ala Asn Thr Arg Tyr Phe Gly Val 35 40 45 IleTrp Asp Ala Ala Gly Gly Gly Ser Phe Ala Val Ile Pro His Glu 50 55 60 AlaSer Gly Lys Thr Thr Ser Val Pro Leu Phe Asn Gly His Lys Ser 65 70 75 80Ala Val Leu Asp Ile Ala Phe His Pro Phe Asn Glu Asn Leu Val Gly 85 90 95Ser Val Ser Glu Asp Cys Asn Ile Cys Ile Trp Gly Ile Pro Glu Gly 100 105110 Gly Leu Thr Asp Ser Ile Ser Thr Pro Leu Gln Thr Leu Ser Gly His 115120 125 Lys Arg Lys Val Gly Thr Ile Ser Phe Gly Pro Val Ala Asp Asn Val130 135 140 Ala Val Thr Ser Ser Gly Asp Phe Leu Val Lys Thr Trp Asp ValGlu 145 150 155 160 Gln Gly Lys Asn Leu Thr Thr Val Glu Gly His Ser AspMet Ile Thr 165 170 175 Ser Cys Glu Trp Asn His Asn Gly Ser Gln Ile ValThr Thr Cys Lys 180 185 190 Asp Lys Lys Ala Arg Val Phe Asp Pro Arg ThrAsn Ser Ile Val Asn 195 200 205 Glu Val Val Cys His Gln Gly Val Lys AsnSer Arg Ala Ile Phe Ala 210 215 220 Lys Asp Lys Val Ile Thr Val Gly PheSer Lys Thr Ser Glu Arg Glu 225 230 235 240 Leu His Ile Tyr Asp Pro ArgAla Phe Thr Thr Pro Leu Ser Ala Gln 245 250 255 Val Val Asp Ser Ala SerGly Leu Leu Met Pro Phe Tyr Asp Ala Asp 260 265 270 Asn Ser Ile Leu TyrLeu Ala Gly Lys Gly Asp Gly Asn Ile Arg Tyr 275 280 285 Tyr Glu Leu ValAsp Glu Ser Pro Tyr Ile His Phe Leu Ser Glu Phe 290 295 300 Lys Ser AlaThr Pro Gln Arg Gly Leu Cys Phe Leu Pro Lys Arg Cys 305 310 315 320 LeuAsn Thr Ser Glu Cys Glu Ile Ala Arg Gly Leu Lys Val Thr Pro 325 330 335Phe Thr Val Glu Pro Ile Ser Phe Arg Val Pro Arg Lys Ser Asp Ile 340 345350 Phe Gln Gly Asp Ile Tyr Pro Asp Thr Tyr Ala Gly Glu Pro Ser Leu 355360 365 Thr Ala Glu Gln Trp Val Ser Gly Thr Asn Ala Glu Pro Lys Thr Val370 375 380 Ser Leu Ala Gly Gly Phe Val Lys Lys Ala Ser Ala Val Glu PheLys 385 390 395 400 Pro Val Val Gln Val Gln Glu Gly Pro Lys Asn Glu LysGlu Leu Arg 405 410 415 Glu Glu Tyr Glu Lys Leu Lys Ile Arg Val Ala TyrLeu Glu Ser Glu 420 425 430 Ile Val Lys Lys Asp Ala Lys Ile Lys Glu LeuThr Asn 435 440 445 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 431 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: CSTF50kDa, Fig. 20 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37: Met Tyr Arg ThrLys Val Gly Leu Lys Asp Arg Gln Gln Leu Tyr Lys 1 5 10 15 Leu Ile IleSer Gln Leu Leu Tyr Asp Gly Tyr Ile Ser Ile Ala Asn 20 25 30 Gly Leu IleAsn Glu Ile Lys Pro Gln Ser Val Cys Ala Pro Ser Glu 35 40 45 Gln Leu LeuHis Leu Ile Lys Leu Gly Met Glu Asn Asp Asp Thr Ala 50 55 60 Val Gln TyrAla Ile Gly Arg Ser Asp Thr Val Ala Pro Gly Thr Gly 65 70 75 80 Ile AspLeu Glu Phe Asp Ala Asp Val Gln Thr Met Ser Pro Glu Ala 85 90 95 Ser GluTyr Glu Thr Cys Tyr Val Thr Ser His Lys Gly Pro Cys Arg 100 105 110 ValAla Thr Tyr Ser Arg Asp Gly Gln Leu Ile Ala Thr Gly Ser Ala 115 120 125Asp Ala Ser Ile Lys Ile Leu Asp Thr Glu Arg Met Leu Ala Lys Ser 130 135140 Ala Met Pro Ile Glu Val Met Met Asn Glu Thr Ala Gln Gln Asn Met 145150 155 160 Glu Asn His Pro Val Ile Arg Thr Leu Tyr Asp His Val Asp GluVal 165 170 175 Thr Cys Leu Ala Phe His Pro Thr Glu Gln Ile Leu Ala SerGly Ser 180 185 190 Arg Asp Tyr Thr Leu Lys Leu Phe Asp Tyr Ser Lys ProSer Ala Lys 195 200 205 Arg Ala Phe Lys Tyr Ile Gln Glu Ala Glu Met LeuArg Ser Ile Ser 210 215 220 Phe His Pro Ser Gly Asp Phe Ile Leu Val GlyThr Gln His Pro Thr 225 230 235 240 Leu Arg Leu Tyr Asp Ile Asn Thr PheGln Cys Phe Val Ser Cys Asn 245 250 255 Pro Gln Asp Gln His Thr Asp AlaIle Cys Ser Val Asn Tyr Asn Ser 260 265 270 Ser Ala Asn Met Tyr Val ThrGly Ser Lys Asp Gly Cys Ile Lys Leu 275 280 285 Trp Asp Gly Val Ser AsnArg Cys Ile Thr Thr Phe Glu Lys Ala His 290 295 300 Asp Gly Ala Glu ValCys Ser Ala Ile Phe Ser Lys Asn Ser Lys Tyr 305 310 315 320 Ile Leu SerSer Gly Lys Asp Ser Val Ala Lys Leu Trp Glu Ile Ser 325 330 335 Thr GlyArg Thr Leu Val Arg Tyr Thr Gly Ala Gly Leu Ser Gly Arg 340 345 350 GlnVal His Arg Thr Gln Ala Val Phe Asn His Thr Glu Asp Tyr Val 355 360 365Leu Leu Pro Asp Glu Arg Thr Ile Ser Leu Cys Cys Trp Asp Ser Arg 370 375380 Thr Ala Glu Arg Arg Asn Leu Leu Ser Leu Gly His Asn Asn Ile Val 385390 395 400 Arg Cys Ile Val His Ser Pro Thr Asn Pro Gly Phe Met Thr CysSer 405 410 415 Asp Asp Phe Arg Ala Arg Phe Trp Tyr Arg Arg Ser Thr ThrAsp 420 425 430 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 340 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta1 bovine, Fig. 21 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: Met Ser GluLeu Asp Gln Leu Arg Gln Glu Ala Glu Gln Leu Lys Asn 1 5 10 15 Gln IleArg Asp Ala Arg Lys Ala Cys Ala Asp Ala Thr Leu Ser Gln 20 25 30 Ile ThrAsn Asn Ile Asp Pro Val Gly Arg Ile Gln Met Arg Thr Arg 35 40 45 Arg ThrLeu Arg Gly His Leu Ala Lys Ile Tyr Ala Met His Trp Gly 50 55 60 Thr AspSer Arg Leu Leu Val Ser Ala Ser Gln Asp Gly Lys Leu Ile 65 70 75 80 IleTrp Asp Ser Tyr Thr Thr Asn Lys Val His Ala Ile Pro Leu Arg 85 90 95 SerSer Trp Val Met Thr Cys Ala Tyr Ala Pro Ser Gly Asn Tyr Val 100 105 110Ala Cys Gly Gly Leu Asp Asn Ile Cys Ser Ile Tyr Asn Leu Lys Thr 115 120125 Arg Glu Gly Asn Val Arg Val Ser Arg Glu Leu Ala Gly His Thr Gly 130135 140 Tyr Leu Ser Cys Cys Arg Phe Leu Asp Asp Asn Gln Ile Val Thr Ser145 150 155 160 Ser Gly Asp Thr Thr Cys Ala Leu Trp Asp Ile Glu Thr GlyGln Gln 165 170 175 Thr Thr Thr Phe Thr Gly His Thr Gly Asp Val Met SerLeu Ser Leu 180 185 190 Ala Pro Asp Thr Arg Leu Phe Val Ser Gly Ala CysAsp Ala Ser Ala 195 200 205 Lys Leu Trp Asp Val Arg Glu Gly Met Cys ArgGln Thr Phe Thr Gly 210 215 220 His Glu Ser Asp Ile Asn Ala Ile Cys PhePhe Pro Asn Gly Asn Ala 225 230 235 240 Phe Ala Thr Gly Ser Asp Asp AlaThr Cys Arg Leu Phe Asp Leu Arg 245 250 255 Ala Asp Gln Glu Leu Met ThrTyr Ser His Asp Asn Ile Ile Cys Gly 260 265 270 Ile Thr Ser Val Ser PheSer Lys Ser Gly Arg Leu Leu Leu Ala Gly 275 280 285 Tyr Asp Asp Phe AsnCys Asn Val Trp Asp Ala Leu Lys Ala Asp Arg 290 295 300 Ala Gly Val LeuAla Gly His Asp Asn Arg Val Ser Cys Leu Gly Val 305 310 315 320 Thr AspAsp Gly Met Ala Val Ala Thr Gly Ser Trp Asp Ser Phe Leu 325 330 335 LysIle Trp Asn 340 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 326 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:G-Beta- bovine (2), Fig. 22 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39: ArgAsn Gln Ile Arg Asp Ala Arg Lys Ala Cys Gly Asp Ser Thr Leu 1 5 10 15Thr Gln Ile Thr Ala Gly Leu Asp Pro Val Gly Arg Ile Gln Met Arg 20 25 30Thr Arg Arg Thr Leu Arg Gly His Leu Ala Lys Ile Tyr Ala Met His 35 40 45Trp Gly Thr Asp Ser Arg Leu Leu Val Ser Ala Ser Gln Asp Gly Lys 50 55 60Leu Ile Ile Trp Asp Ser Glu Gly Asn Val Arg Tyr Thr Thr Asn Lys 65 70 7580 Val His Ala Ile Pro Leu Arg Ser Ser Trp Val Met Thr Cys Ala Tyr 85 9095 Ala Pro Ser Gly Asn Phe Val Ala Cys Gly Gly Leu Asp Asn Ile Cys 100105 110 Ser Ile Tyr Ser Leu Lys Thr Arg Val Ser Arg Glu Leu Pro Gly His115 120 125 Thr Gly Tyr Leu Ser Cys Cys Arg Phe Leu Asp Asp Asn Gln IleIle 130 135 140 Thr Ser Ser Gly Asp Thr Thr Cys Ala Leu Trp Asp Ile GluThr Gly 145 150 155 160 Gln Gln Thr Val Gly Phe Ala Gly His Ser Gly AspVal Met Ser Leu 165 170 175 Ser Leu Ala Pro Asp Gly Arg Thr Phe Val SerGly Ala Cys Asp Ala 180 185 190 Ser Ile Lys Leu Trp Asp Val Arg Asp SerMet Cys Arg Gln Thr Phe 195 200 205 Ile Gly His Glu Ser Asp Ile Asn AlaVal Ala Phe Phe Pro Asn Gly 210 215 220 Tyr Ala Phe Thr Thr Gly Ser AspAsp Ala Thr Cys Arg Leu Phe Asp 225 230 235 240 Leu Arg Ala Asp Gln GluLeu Leu Met Tyr Ser His Asp Asn Ile Ile 245 250 255 Cys Gly Ile Thr SerVal Ala Phe Ser Arg Ser Gly Arg Leu Leu Leu 260 265 270 Ala Gly Tyr AspAsp Phe Asn Cys Asn Ile Trp Asp Ala Met Lys Gly 275 280 285 Asp Arg AlaGly Val Leu Ala Gly His Asp Asn Arg Val Ser Cys Leu 290 295 300 Gly ValThr Asp Asp Gly Met Ala Val Ala Thr Gly Ser Trp Asp Ser 305 310 315 320Phe Leu Lys Ile Trp Asn 325 (2) INFORMATION FOR SEQ ID NO:40: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 340 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G- BETA DROSOPH, Fig. 23 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:40: Met Asn Glu Leu Asp Ser Leu Arg Gln Glu Ala Glu Ser LeuLys Asn 1 5 10 15 Ala Ile Arg Asp Ala Arg Lys Ala Ala Cys Asp Thr SerLeu Leu Gln 20 25 30 Ala Ala Thr Ser Leu Glu Pro Ile Gly Arg Ile Gln MetArg Thr Arg 35 40 45 Arg Thr Leu Arg Gly His Leu Ala Lys Ile Tyr Ala MetHis Trp Gly 50 55 60 Asn Asp Ser Arg Asn Leu Val Ser Ala Ser Gln Asp GlyLys Leu Ile 65 70 75 80 Val Trp Asp Ser His Thr Thr Asn Lys Val His AlaIle Pro Leu Arg 85 90 95 Ser Ser Trp Val Met Thr Cys Ala Tyr Ala Pro SerGly Ser Tyr Val 100 105 110 Ala Cys Gly Gly Leu Asp Asn Met Cys Ser IleTyr Asn Leu Lys Thr 115 120 125 Arg Glu Gly Asn Val Arg Val Ser Arg GluLeu Pro Gly His Gly Gly 130 135 140 Tyr Leu Ser Cys Cys Arg Phe Leu AspAsp Asn Gln Ile Val Thr Ser 145 150 155 160 Ser Gly Asp Met Ser Cys GlyLeu Trp Asp Ile Glu Thr Gly Leu Gln 165 170 175 Val Thr Ser Phe Leu GlyHis Thr Gly Asp Val Met Ala Leu Ser Leu 180 185 190 Ala Pro Gln Cys LysThr Phe Val Ser Gly Ala Cys Asp Ala Ser Ala 195 200 205 Lys Leu Trp AspIle Arg Glu Gly Val Cys Lys Gln Thr Phe Pro Gly 210 215 220 His Glu SerAsp Ile Asn Ala Val Thr Phe Phe Pro Asn Gly Gln Ala 225 230 235 240 PheAla Thr Gly Ser Asp Asp Ala Thr Cys Arg Leu Phe Asp Ile Arg 245 250 255Ala Asp Gln Glu Leu Ala Met Tyr Ser His Asp Asn Ile Ile Cys Gly 260 265270 Ile Thr Ser Val Ala Phe Ser Lys Ser Gly Arg Leu Leu Leu Ala Gly 275280 285 Tyr Asp Asp Phe Asn Cys Asn Val Trp Asp Thr Met Lys Ala Glu Arg290 295 300 Ser Gly Ile Leu Ala Gly His Asp Asn Arg Val Ser Cys Leu GlyVal 305 310 315 320 Thr Glu Asn Gly Met Ala Val Ala Thr Gly Ser Trp AspSer Phe Leu 325 330 335 Arg Val Trp Asn 340 (2) INFORMATION FOR SEQ IDNO:41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 317 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-BETA HUMAN, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQID NO:41: Met Thr Glu Gln Met Thr Leu Arg Gly Thr Leu Lys Gly His AsnGly 1 5 10 15 Trp Val Thr Gln Ile Ala Thr Thr Pro Gln Phe Pro Asp MetIle Leu 20 25 30 Ser Ala Ser Arg Asp Lys Thr Ile Ile Met Trp Lys Leu ThrArg Asp 35 40 45 Glu Thr Asn Tyr Gly Ile Pro Gln Arg Ala Leu Arg Gly HisSer His 50 55 60 Phe Val Ser Asp Val Val Ile Ser Ser Asp Gly Gln Phe AlaLeu Ser 65 70 75 80 Gly Ser Trp Asp Gly Thr Leu Arg Leu Trp Asp Leu ThrThr Gly Thr 85 90 95 Thr Thr Arg Arg Phe Val Gly His Thr Lys Asp Val LeuSer Val Ala 100 105 110 Phe Ser Ser Asp Asn Arg Gln Ile Val Ser Gly SerArg Asp Lys Thr 115 120 125 Ile Lys Leu Trp Asn Thr Leu Gly Val Cys LysTyr Thr Val Gln Asp 130 135 140 Glu Ser His Ser Glu Trp Val Ser Cys ValArg Phe Ser Pro Asn Ser 145 150 155 160 Ser Asn Pro Ile Ile Val Ser CysGly Trp Asp Lys Leu Val Lys Val 165 170 175 Trp Asn Leu Ala Asn Cys LysLeu Lys Thr Asn His Ile Gly His Thr 180 185 190 Gly Tyr Leu Asn Thr ValThr Val Ser Pro Asp Gly Ser Leu Cys Ala 195 200 205 Ser Gly Gly Lys AspGly Gln Ala Met Leu Trp Asp Leu Asn Glu Gly 210 215 220 Lys His Leu TyrThr Leu Asp Gly Gly Asp Ile Ile Asn Ala Leu Cys 225 230 235 240 Phe SerPro Asn Arg Tyr Trp Leu Cys Ala Ala Thr Gly Pro Ser Ile 245 250 255 LysIle Trp Asp Leu Glu Gly Lys Ile Ile Val Asp Glu Leu Lys Gln 260 265 270Glu Val Ile Ser Thr Ser Ser Lys Ala Glu Pro Pro Gln Cys Thr Ser 275 280285 Leu Ala Trp Ser Ala Asp Gly Gln Thr Leu Phe Ala Gly Tyr Thr Asp 290295 300 Asn Leu Val Arg Val Trp Gln Val Thr Ile Gly Thr Arg 305 310 315(2) INFORMATION FOR SEQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 340 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta 2 (Human), Fig. 25 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:42: Met Ser Glu Leu Glu Gln Leu Arg GlnGlu Ala Glu Gln Leu Arg Asn 1 5 10 15 Gln Ile Arg Asp Ala Arg Lys AlaCys Gly Asp Ser Thr Leu Thr Gln 20 25 30 Ile Thr Ala Gly Leu Asp Pro ValGly Arg Ile Gln Met Arg Thr Arg 35 40 45 Arg Thr Leu Arg Gly His Leu AlaLys Ile Tyr Ala Met His Trp Gly 50 55 60 Thr Asp Ser Arg Leu Leu Val SerAla Ser Gln Asp Gly Lys Leu Ile 65 70 75 80 Ile Trp Asp Ser Tyr Thr ThrAsn Lys Val His Ala Ile Pro Leu Arg 85 90 95 Ser Ser Trp Val Met Thr CysAla Tyr Ala Pro Ser Gly Asn Phe Val 100 105 110 Ala Cys Gly Gly Leu AspAsn Ile Cys Ser Ile Tyr Ser Leu Lys Thr 115 120 125 Arg Glu Gly Asn ValArg Val Ser Arg Glu Leu Pro Gly His Thr Gly 130 135 140 Tyr Leu Ser CysCys Arg Phe Leu Asp Asp Asn Gln Ile Ile Thr Ser 145 150 155 160 Ser GlyAsp Thr Thr Cys Ala Leu Trp Asp Ile Glu Thr Gly Gln Gln 165 170 175 ThrVal Gly Phe Ala Gly His Ser Gly Asp Val Met Ser Leu Ser Leu 180 185 190Ala Pro Asp Gly Arg Thr Phe Val Ser Gly Ala Cys Asp Ala Ser Ile 195 200205 Lys Leu Trp Asp Val Arg Asp Ser Met Cys Arg Gln Thr Phe Ile Gly 210215 220 His Glu Ser Asp Ile Asn Ala Val Ala Phe Phe Pro Asn Gly Tyr Ala225 230 235 240 Phe Thr Thr Gly Ser Asp Asp Ala Thr Cys Arg Leu Phe AspLeu Arg 245 250 255 Ala Asp Gln Glu Leu Leu Met Tyr Ser His Asp Asn IleIle Cys Gly 260 265 270 Ile Thr Ser Val Ala Phe Ser Arg Ser Gly Arg LeuLeu Leu Ala Gly 275 280 285 Tyr Asp Asp Phe Asn Cys Asn Ile Trp Asp AlaMet Lys Gly Asp Arg 290 295 300 Ala Gly Val Leu Ala Gly His Asp Asn ArgVal Ser Cys Leu Gly Val 305 310 315 320 Thr Asp Asp Gly Met Ala Val AlaThr Gly Ser Trp Asp Ser Phe Leu 325 330 335 Lys Ile Trp Asn 340 (2)INFORMATION FOR SEQ ID NO:43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: G-Beta 4 (mouse), Fig. 26 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:43: Lys Lys Asx Glu Thr Asx Val Asn Met Gly ArgTyr Thr Pro Arg Ile 1 5 10 15 Lys His Ile Lys Arg Pro Arg Arg Thr AspXaa Xaa Gly 20 25 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 718 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:GROUCHO PROTEIN DROSOPH, Fig. 27 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:44: Met Tyr Pro Ser Pro Val Arg His Pro Ala Ala Gly Gly Pro Pro Pro 15 10 15 Gln Gly Pro Ile Lys Phe Thr Ile Ala Asp Thr Leu Glu Arg Ile Lys20 25 30 Glu Glu Phe Asn Phe Leu Gln Ala His Tyr His Ser Ile Lys Leu Glu35 40 45 Cys Glu Lys Leu Ser Asn Glu Lys Thr Glu Met Gln Arg His Tyr Val50 55 60 Met Tyr Tyr Glu Met Ser Tyr Gly Leu Asn Val Glu Met His Lys Gln65 70 75 80 Thr Glu Ile Ala Lys Arg Leu Asn Thr Leu Ile Asn Gln Leu LeuPro 85 90 95 Phe Leu Gln Ala Asp His Gln Gln Gln Val Leu Gln Ala Val GluArg 100 105 110 Ala Lys Gln Val Thr Met Gln Glu Leu Asn Leu Ile Ile GlyGln Gln 115 120 125 Ile His Ala Gln Gln Val Pro Gly Gly Pro Pro Gln ProMet Gly Ala 130 135 140 Leu Asn Pro Phe Gly Ala Leu Gly Ala Thr Met GlyLeu Pro His Gly 145 150 155 160 Pro Gln Gly Leu Leu Asn Lys Pro Pro GluHis His Arg Pro Asp Ile 165 170 175 Lys Pro Thr Gly Leu Glu Gly Pro AlaAla Ala Glu Glu Arg Leu Arg 180 185 190 Asn Ser Val Ser Pro Ala Asp ArgGlu Lys Tyr Arg Thr Arg Ser Pro 195 200 205 Leu Asp Ile Glu Asn Asp SerLys Arg Arg Lys Asp Glu Lys Leu Gln 210 215 220 Glu Asp Glu Gly Glu LysSer Asp Gln Asp Leu Val Val Asp Val Ala 225 230 235 240 Asn Glu Met GluSer His Ser Pro Arg Pro Asn Gly Glu His Val Ser 245 250 255 Met Glu ValArg Asp Arg Glu Ser Leu Asn Gly Glu Arg Leu Glu Lys 260 265 270 Pro SerSer Ser Gly Ile Lys Gln Glu Arg Pro Pro Ser Arg Ser Gly 275 280 285 SerSer Ser Ser Arg Ser Thr Pro Ser Leu Lys Thr Lys Asp Met Glu 290 295 300Lys Pro Gly Thr Pro Gly Ala Lys Ala Arg Thr Pro Thr Pro Asn Ala 305 310315 320 Ala Ala Pro Ala Pro Gly Val Asn Pro Lys Gln Met Met Pro Gln Gly325 330 335 Pro Pro Pro Ala Gly Tyr Pro Gly Ala Pro Tyr Gln Arg Pro AlaAsp 340 345 350 Pro Tyr Gln Arg Pro Pro Ser Asp Pro Ala Tyr Gly Arg ProPro Pro 355 360 365 Met Pro Tyr Asp Pro His Ala His Val Arg Thr Asn GlyIle Pro His 370 375 380 Pro Ser Ala Leu Thr Gly Gly Lys Pro Ala Tyr SerPhe His Met Asn 385 390 395 400 Gly Glu Gly Ser Leu Gln Pro Val Pro PhePro Pro Asp Ala Leu Val 405 410 415 Gly Val Gly Ile Pro Arg His Ala ArgGln Ile Asn Thr Leu Ser His 420 425 430 Gly Glu Val Val Cys Ala Val ThrIle Ser Asn Pro Thr Lys Tyr Val 435 440 445 Tyr Thr Gly Gly Lys Gly CysVal Lys Val Trp Asp Ile Ser Gln Pro 450 455 460 Gly Asn Lys Asn Pro ValSer Gln Leu Asp Cys Leu Gln Arg Asp Asn 465 470 475 480 Tyr Ile Arg SerVal Lys Leu Leu Pro Asp Gly Arg Thr Leu Ile Val 485 490 495 Gly Gly GluAla Ser Asn Leu Ser Ile Trp Asp Leu Ala Ser Pro Thr 500 505 510 Pro ArgIle Lys Ala Glu Leu Thr Ser Ala Ala Pro Ala Cys Tyr Ala 515 520 525 LeuAla Ser Pro Asp Ser Lys Val Cys Phe Ser Cys Cys Ser Asp Gly 530 535 540Asn Ile Ala Val Trp Asp Leu His Asn Glu Ile Leu Val Arg Gln Phe 545 550555 560 Gln Gly His Thr Asp Gly Ala Ser Cys Ile Asp Ile Ser Pro Asp Gly565 570 575 Ser Arg Leu Trp Thr Gly Gly Leu Asp Asn Thr Val Arg Ser TrpAsp 580 585 590 Leu Arg Glu Gly Arg Gln Leu Gln Gln His Asp Phe Ser SerGln Ile 595 600 605 Phe Ser Leu Gly Tyr Cys Pro Thr Gly Asp Trp Leu AlaVal Gly Met 610 615 620 Glu Asn Ser His Val Glu Val Leu His Ala Ser LysPro Asp Lys Tyr 625 630 635 640 Gln Leu His Leu His Glu Ser Cys Val LeuSer Leu Arg Phe Ala Ala 645 650 655 Cys Gly Lys Trp Phe Val Ser Thr GlyLys Asp Asn Leu Leu Asn Ala 660 665 670 Trp Arg Thr Pro Tyr Gly Ala SerIle Phe Gln Ser Lys Glu Thr Ser 675 680 685 Ser Val Leu Ser Cys Asp IleSer Thr Asp Asp Lys Tyr Ile Val Thr 690 695 700 Gly Ser Gly Asp Lys LysAla Thr Val Tyr Glu Val Ile Tyr 705 710 715 (2) INFORMATION FOR SEQ IDNO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 341 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GTP binding protein (squid), Fig. 28 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:45: Met Thr Ser Glu Leu Glu Ala Leu Arg Gln GluThr Glu Gln Leu Lys 1 5 10 15 Asn Gln Ile Arg Glu Ala Arg Lys Ala AlaAla Asp Thr Thr Leu Ala 20 25 30 Met Ala Thr Ala Asn Val Glu Pro Val GlyArg Ile Gln Met Arg Thr 35 40 45 Arg Arg Thr Leu Arg Gly His Leu Ala LysIle Tyr Ala Met His Trp 50 55 60 Ala Ser Asp Ser Arg Asn Leu Val Ser AlaSer Gln Asp Gly Lys Leu 65 70 75 80 Ile Val Trp Asp Gly Tyr Thr Thr AsnLys Val His Ala Ile Pro Leu 85 90 95 Arg Ser Ser Trp Val Met Thr Cys AlaTyr Ala Pro Ser Gly Asn Tyr 100 105 110 Val Ala Cys Gly Gly Leu Asp AsnIle Cys Ser Ile Tyr Ser Leu Lys 115 120 125 Thr Arg Glu Gly Asn Val ArgVal Ser Arg Glu Leu Pro Gly His Thr 130 135 140 Gly Tyr Leu Ser Cys CysArg Phe Ile Asp Asp Asn Gln Ile Val Thr 145 150 155 160 Ser Ser Gly AspMet Thr Cys Ala Leu Trp Asn Ile Glu Thr Gly Asn 165 170 175 Gln Ile ThrSer Phe Gly Gly His Thr Gly Asp Val Met Ser Leu Ser 180 185 190 Leu AlaPro Asp Met Arg Thr Phe Val Ser Gly Ala Cys Asp Ala Ser 195 200 205 AlaLys Leu Phe Asp Ile Arg Asp Gly Ile Cys Lys Gln Thr Phe Thr 210 215 220Gly His Glu Ser Asp Ile Asn Ala Ile Thr Tyr Phe Pro Asn Gly Phe 225 230235 240 Ala Phe Ala Thr Gly Ser Asp Asp Ala Thr Cys Arg Leu Phe Asp Ile245 250 255 Arg Ala Asp Gln Glu Ile Gly Met Tyr Ser His Asp Asn Ile IleCys 260 265 270 Gly Ile Thr Ser Val Ala Phe Ser Lys Ser Gly Arg Leu LeuLeu Gly 275 280 285 Gly Tyr Asp Asp Phe Asn Cys Asn Val Trp Asp Val LeuLys Gln Glu 290 295 300 Arg Ala Gly Val Leu Ala Gly His Asp Asn Arg ValSer Cys Leu Gly 305 310 315 320 Val Thr Glu Asp Gly Met Ala Val Ala ThrGly Ser Trp Asp Ser Phe 325 330 335 Leu Lys Ile Trp Asn 340 (2)INFORMATION FOR SEQ ID NO:46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:410 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: IEF SSP 9306, Fig. 29 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:46: Met Ala Asp Lys Glu Ala Ala Phe Asp Asp AlaVal Glu Glu Arg Val 1 5 10 15 Ile Asn Glu Glu Tyr Lys Ile Trp Lys LysAsn Thr Pro Phe Leu Tyr 20 25 30 Asp Leu Val Met Thr His Ala Leu Glu TrpPro Ser Leu Thr Ala Gln 35 40 45 Trp Leu Pro Asp Val Thr Arg Pro Glu GlyLys Asp Phe Ser Ile His 50 55 60 Arg Leu Val Leu Gly Thr His Thr Ser AspGlu Gln Asn His Leu Val 65 70 75 80 Ile Ala Ser Val Gln Leu Pro Asn AspAsp Ala Gln Phe Asp Ala Ser 85 90 95 His Tyr Asp Ser Glu Lys Gly Glu PheGly Gly Phe Gly Ser Val Ser 100 105 110 Gly Lys Ile Glu Ile Glu Ile LysIle Asn His Glu Gly Glu Val Asn 115 120 125 Arg Ala Arg Tyr Met Pro GlnAsn Pro Cys Ile Ile Ala Thr Lys Thr 130 135 140 Pro Ser Ser Asp Val LeuVal Phe Asp Tyr Thr Lys His Pro Ser Lys 145 150 155 160 Pro Asp Pro SerGly Glu Cys Asn Pro Asp Leu Arg Leu Arg Gly His 165 170 175 Gln Lys GluGly Tyr Gly Leu Ser Trp Asn Pro Asn Leu Ser Gly His 180 185 190 Leu LeuSer Ala Ser Asp Asp His Thr Ile Cys Leu Trp Asp Ile Ser 195 200 205 AlaVal Pro Lys Glu Gly Lys Val Val Asp Ala Lys Thr Ile Phe Thr 210 215 220Gly His Thr Ala Val Val Glu Asp Val Ser Trp His Leu Leu His Glu 225 230235 240 Ser Leu Phe Gly Ser Val Ala Asp Asp Gln Lys Leu Met Ile Trp Asp245 250 255 Thr Arg Ser Asn Asn Thr Ser Lys Pro Ser His Ser Val Asp AlaHis 260 265 270 Thr Ala Glu Val Asn Cys Leu Ser Phe Asn Pro Tyr Ser GluPhe Ile 275 280 285 Leu Ala Thr Gly Ser Ala Asp Lys Thr Val Ala Leu TrpAsp Leu Arg 290 295 300 Asn Leu Lys Leu Lys Leu His Ser Phe Glu Ser HisLys Asp Glu Ile 305 310 315 320 Phe Gln Val Gln Trp Ser Pro His Asn GluThr Ile Leu Ala Ser Ser 325 330 335 Gly Thr Asp Arg Arg Leu Asn Val TrpAsp Leu Ser Lys Ile Gly Glu 340 345 350 Glu Gln Ser Pro Glu Asp Ala GluAsp Gly Pro Pro Glu Leu Leu Phe 355 360 365 Ile His Gly Gly His Thr AlaLys Ile Ser Asp Phe Ser Trp Asn Pro 370 375 380 Asn Glu Pro Trp Val IleCys Ser Val Ser Glu Asp Asn Ile Met Gln 385 390 395 400 Val Trp Gln MetGlu Leu Val Leu Asp His 405 410 (2) INFORMATION FOR SEQ ID NO:47: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 317 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: HUMAN 12.3, Fig. 30 (xi) SEQUENCE DESCRIPTION: SEQID NO:47: Met Thr Glu Gln Met Thr Leu Arg Gly Thr Leu Lys Gly His AsnGly 1 5 10 15 Trp Val Thr Gln Ile Ala Thr Thr Pro Gln Phe Pro Asp MetIle Leu 20 25 30 Ser Ala Ser Arg Asp Lys Thr Ile Ile Met Trp Lys Leu ThrArg Asp 35 40 45 Glu Thr Asn Tyr Gly Ile Pro Gln Arg Ala Leu Arg Gly HisSer His 50 55 60 Phe Val Ser Asp Val Val Ile Ser Ser Asp Gly Gln Phe AlaLeu Ser 65 70 75 80 Gly Ser Trp Asp Gly Thr Leu Arg Leu Trp Asp Leu ThrThr Gly Thr 85 90 95 Thr Thr Arg Arg Phe Val Gly His Thr Lys Asp Val LeuSer Val Ala 100 105 110 Phe Ser Ser Asp Asn Arg Gln Ile Val Ser Gly SerArg Asp Lys Thr 115 120 125 Ile Lys Leu Trp Asn Thr Leu Gly Val Cys LysTyr Thr Val Gln Asp 130 135 140 Glu Ser His Ser Glu Trp Val Ser Cys ValArg Phe Ser Pro Asn Ser 145 150 155 160 Ser Asn Pro Ile Ile Val Ser CysGly Trp Asp Lys Leu Val Lys Val 165 170 175 Trp Asn Leu Ala Asn Cys LysLeu Lys Thr Asn His Ile Gly His Thr 180 185 190 Gly Tyr Leu Asn Thr ValThr Val Ser Pro Asp Gly Ser Leu Cys Ala 195 200 205 Ser Gly Gly Lys AspGly Gln Ala Met Leu Trp Asp Leu Asn Glu Gly 210 215 220 Lys His Leu TyrThr Leu Asp Gly Gly Asp Ile Ile Asn Ala Leu Cys 225 230 235 240 Phe SerPro Asn Arg Tyr Trp Leu Cys Ala Ala Thr Gly Pro Ser Ile 245 250 255 LysIle Trp Asp Leu Glu Gly Lys Ile Ile Val Asp Glu Leu Lys Gln 260 265 270Glu Val Ile Ser Thr Ser Ser Lys Ala Glu Pro Pro Gln Cys Thr Ser 275 280285 Leu Ala Trp Ser Ala Asp Gly Gln Thr Leu Phe Ala Gly Tyr Thr Asp 290295 300 Asn Leu Val Arg Val Trp Gln Val Thr Ile Gly Thr Arg 305 310 315(2) INFORMATION FOR SEQ ID NO:48: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 425 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: IEF -7442 - human, Fig. 31 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:48: Met Ala Ser Lys Glu Met Phe Glu AspThr Val Glu Glu Arg Val Ile 1 5 10 15 Asn Glu Glu Tyr Lys Ile Trp LysLys Asn Thr Pro Phe Leu Tyr Asp 20 25 30 Leu Val Met Thr His Ala Leu GlnTrp Pro Ser Leu Thr Val Gln Trp 35 40 45 Leu Pro Glu Val Thr Lys Pro GluGly Lys Asp Tyr Ala Leu His Trp 50 55 60 Leu Val Leu Gly Thr His Thr SerAsp Glu Gln Asn His Leu Val Val 65 70 75 80 Ala Arg Val His Ile Pro AsnAsp Asp Ala Gln Phe Asp Ala Ser His 85 90 95 Cys Asp Ser Asp Lys Gly GluPhe Gly Gly Phe Gly Ser Val Thr Gly 100 105 110 Lys Ile Glu Cys Glu IleLys Ile Asn His Glu Gly Glu Val Asn Arg 115 120 125 Ala Arg Tyr Met ProGln Asn Pro His Ile Ile Ala Thr Lys Thr Pro 130 135 140 Ser Ser Asp ValLeu Val Phe Asp Tyr Thr Lys His Pro Ala Lys Pro 145 150 155 160 Asp ProSer Gly Glu Cys Asn Pro Asp Leu Arg Leu Arg Gly His Gln 165 170 175 LysGlu Gly Tyr Gly Leu Ser Trp Asn Ser Asn Leu Ser Gly His Leu 180 185 190Leu Ser Ala Ser Asp Asp His Thr Val Cys Leu Trp Asp Ile Asn Ala 195 200205 Gly Pro Lys Glu Gly Lys Ile Val Asp Ala Lys Ala Ile Phe Thr Gly 210215 220 His Ser Ala Val Val Glu Asp Val Ala Trp His Leu Leu His Glu Ser225 230 235 240 Leu Phe Gly Ser Val Ala Asp Asp Gln Lys Leu Met Ile TrpAsp Thr 245 250 255 Arg Ser Asn Thr Thr Ser Lys Pro Ser His Leu Val AspAla His Thr 260 265 270 Ala Glu Val Asn Cys Leu Ser Phe Asn Pro Tyr SerGlu Phe Ile Leu 275 280 285 Ala Thr Gly Ser Ala Asp Lys Thr Val Ala LeuTrp Asp Leu Arg Asn 290 295 300 Leu Lys Leu Lys Leu His Thr Phe Glu SerHis Lys Asp Glu Ile Phe 305 310 315 320 Gln Val His Trp Ser Pro His AsnGlu Thr Ile Leu Ala Ser Ser Gly 325 330 335 Thr Asp Arg Arg Leu Asn ValTrp Asp Leu Ser Lys Ile Gly Glu Glu 340 345 350 Gln Ser Ala Glu Asp AlaGlu Asp Gly Pro Pro Glu Leu Leu Phe Ile 355 360 365 His Gly Gly His ThrAla Lys Ile Ser Asp Phe Ser Trp Asn Pro Asn 370 375 380 Glu Pro Trp ValIle Cys Ser Val Ser Glu Asp Asn Ile Met Gln Ile 385 390 395 400 Trp GlnMet Ala Glu Asn Ile Tyr Asn Asp Glu Glu Ser Asp Val Thr 405 410 415 ThrSer Glu Leu Glu Gly Gln Gly Ser 420 425 (2) INFORMATION FOR SEQ IDNO:49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 605 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Insulin-like growth factor binding protein complex,Fig. 32 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49: Met Ala Leu Arg Lys GlyGly Leu Ala Leu Ala Leu Leu Leu Leu Ser 1 5 10 15 Trp Val Ala Leu GlyPro Arg Ser Leu Glu Gly Ala Asp Pro Gly Thr 20 25 30 Pro Gly Glu Ala GluGly Pro Ala Cys Pro Ala Ala Cys Val Cys Ser 35 40 45 Tyr Asp Asp Asp AlaAsp Glu Leu Ser Val Phe Cys Ser Ser Arg Asn 50 55 60 Leu Thr Arg Leu ProAsp Gly Val Pro Gly Gly Thr Gln Ala Leu Trp 65 70 75 80 Leu Asp Gly AsnAsn Leu Ser Ser Val Pro Pro Ala Ala Phe Gln Asn 85 90 95 Leu Ser Ser LeuGly Phe Leu Asn Leu Gln Gly Gly Gln Leu Gly Ser 100 105 110 Leu Glu ProGln Ala Leu Leu Gly Leu Glu Asn Leu Cys His Leu His 115 120 125 Leu GluArg Asn Gln Leu Arg Ser Leu Ala Leu Gly Thr Phe Ala His 130 135 140 ThrPro Ala Leu Ala Ser Leu Gly Leu Ser Asn Asn Arg Leu Ser Arg 145 150 155160 Leu Glu Asp Gly Leu Phe Glu Gly Leu Gly Ser Leu Trp Asp Leu Asn 165170 175 Leu Gly Trp Asn Ser Leu Ala Val Leu Pro Asp Ala Ala Phe Arg Gly180 185 190 Leu Gly Ser Leu Arg Glu Leu Val Leu Ala Gly Asn Arg Leu AlaTyr 195 200 205 Leu Gln Pro Ala Leu Phe Ser Gly Leu Ala Glu Leu Arg GluLeu Asp 210 215 220 Leu Ser Arg Asn Ala Leu Arg Ala Ile Lys Ala Asn ValPhe Val Gln 225 230 235 240 Leu Pro Arg Leu Gln Lys Leu Tyr Leu Asp ArgAsn Leu Ile Ala Ala 245 250 255 Val Ala Pro Gly Ala Phe Leu Gly Leu LysAla Leu Arg Trp Leu Asp 260 265 270 Leu Ser His Asn Arg Val Ala Gly LeuLeu Glu Asp Thr Phe Pro Gly 275 280 285 Leu Leu Gly Leu Arg Val Leu ArgLeu Ser His Asn Ala Ile Ala Ser 290 295 300 Leu Arg Pro Arg Thr Phe LysAsp Leu His Phe Leu Glu Glu Leu Gln 305 310 315 320 Leu Gly His Asn ArgIle Arg Gln Leu Ala Glu Arg Ser Phe Glu Gly 325 330 335 Leu Gly Gln LeuGlu Val Leu Thr Leu Asp His Asn Gln Leu Gln Glu 340 345 350 Val Lys AlaGly Ala Phe Leu Gly Leu Thr Asn Val Ala Val Met Asn 355 360 365 Leu SerGly Asn Cys Leu Arg Asn Leu Pro Glu Gln Val Phe Arg Gly 370 375 380 LeuGly Lys Leu His Ser Leu His Leu Glu Gly Ser Cys Leu Gly Arg 385 390 395400 Ile Arg Pro His Thr Phe Thr Gly Leu Ser Gly Leu Arg Arg Leu Phe 405410 415 Leu Lys Asp Asn Gly Leu Val Gly Ile Glu Glu Gln Ser Leu Trp Gly420 425 430 Leu Ala Glu Leu Leu Glu Leu Asp Leu Thr Ser Asn Gln Leu ThrHis 435 440 445 Leu Pro His Arg Leu Phe Gln Gly Leu Gly Lys Leu Glu TyrLeu Leu 450 455 460 Leu Ser Arg Asn Arg Leu Ala Glu Leu Pro Ala Asp AlaLeu Gly Pro 465 470 475 480 Leu Gln Arg Ala Phe Trp Leu Asp Val Ser HisAsn Arg Leu Glu Ala 485 490 495 Leu Pro Asn Ser Leu Leu Ala Pro Leu GlyArg Leu Arg Tyr Leu Ser 500 505 510 Leu Arg Asn Asn Ser Leu Arg Thr PheThr Pro Gln Pro Pro Gly Leu 515 520 525 Glu Arg Leu Trp Leu Glu Gly AsnPro Trp Asp Cys Gly Cys Pro Leu 530 535 540 Lys Ala Leu Arg Asp Phe AlaLeu Gln Asn Pro Ser Ala Val Pro Arg 545 550 555 560 Phe Val Gln Ala IleCys Glu Gly Asp Asp Cys Gln Pro Pro Ala Tyr 565 570 575 Thr Tyr Asn AsnIle Thr Cys Ala Ser Pro Pro Glu Val Val Gly Leu 580 585 590 Asp Leu ArgAsp Leu Ser Glu Ala His Phe Ala Pro Cys 595 600 605 (2) INFORMATION FORSEQ ID NO:50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 603 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Insulin-like growth factor bind. pro. complex-rat,Fig. 33 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50: Met Ala Leu Arg Thr GlyGly Pro Ala Leu Val Val Leu Leu Ala Phe 1 5 10 15 Trp Val Ala Leu GlyPro Cys His Leu Gln Gly Thr Asp Pro Gly Ala 20 25 30 Ser Ala Asp Ala GluGly Pro Gln Cys Pro Val Ala Cys Thr Cys Ser 35 40 45 His Asp Asp Tyr ThrAsp Glu Leu Ser Val Phe Cys Ser Ser Lys Asn 50 55 60 Leu Thr His Leu ProAsp Asp Ile Pro Val Ser Thr Arg Ala Leu Trp 65 70 75 80 Leu Asp Gly AsnAsn Leu Ser Ser Ile Pro Ser Ala Ala Phe Gln Asn 85 90 95 Leu Ser Ser LeuAsp Phe Leu Asn Leu Gln Gly Ser Trp Leu Arg Ser 100 105 110 Leu Glu ProGln Ala Leu Leu Gly Leu Gln Asn Leu Tyr Tyr Leu His 115 120 125 Leu GluArg Asn Arg Leu Arg Asn Leu Ala Val Gly Leu Phe Thr His 130 135 140 ThrPro Ser Leu Ala Ser Leu Ser Leu Ser Ser Asn Leu Leu Gly Arg 145 150 155160 Leu Glu Glu Gly Leu Phe Gln Gly Leu Ser His Leu Trp Asp Leu Asn 165170 175 Leu Gly Trp Asn Ser Leu Val Val Leu Pro Asp Thr Val Phe Gln Gly180 185 190 Leu Gly Asn Leu His Glu Leu Val Leu Ala Gly Asn Lys Leu ThrTyr 195 200 205 Leu Gln Pro Ala Leu Phe Cys Gly Leu Gly Glu Leu Arg GluLeu Asp 210 215 220 Leu Ser Arg Asn Ala Leu Arg Ser Val Lys Ala Asn ValPhe Val His 225 230 235 240 Leu Pro Arg Leu Gln Lys Leu Tyr Leu Asp ArgAsn Leu Ile Thr Ala 245 250 255 Val Ala Pro Gly Ala Phe Leu Gly Met LysAla Leu Arg Trp Leu Asp 260 265 270 Leu Ser His Asn Arg Val Ala Gly LeuMet Glu Asp Thr Phe Pro Gly 275 280 285 Leu Leu Gly Leu His Val Leu ArgLeu Ala His Asn Ala Ile Ala Ser 290 295 300 Leu Arg Pro Arg Thr Phe LysAsp Leu His Phe Leu Glu Glu Leu Gln 305 310 315 320 Leu Gly His Asn ArgIle Arg Gln Leu Gly Glu Arg Thr Phe Glu Gly 325 330 335 Leu Gly Gln LeuGlu Val Leu Thr Leu Asn Asp Asn Gln Ile Thr Glu 340 345 350 Val Arg ValGly Ala Phe Ser Gly Leu Phe Asn Val Ala Val Met Asn 355 360 365 Leu SerGly Asn Cys Leu Arg Ser Leu Pro Glu Arg Val Phe Gln Gly 370 375 380 LeuAsp Lys Leu His Ser Leu His Leu Glu His Ser Cys Leu Gly His 385 390 395400 Val Arg Leu His Thr Phe Ala Gly Leu Ser Gly Leu Arg Arg Leu Phe 405410 415 Leu Arg Asp Asn Ser Ile Ser Ser Ile Glu Glu Gln Ser Leu Ala Gly420 425 430 Leu Ser Glu Leu Leu Glu Leu Asp Leu Thr Thr Asn Arg Leu ThrHis 435 440 445 Leu Pro Arg Gln Leu Phe Gln Gly Leu Gly His Leu Glu TyrLeu Leu 450 455 460 Leu Ser Tyr Asn Gln Leu Thr Thr Leu Ser Ala Glu ValLeu Gly Pro 465 470 475 480 Leu Gln Arg Ala Phe Trp Leu Asp Ile Ser HisAsn His Leu Glu Thr 485 490 495 Leu Ala Glu Gly Leu Phe Ser Ser Leu GlyArg Val Arg Tyr Leu Ser 500 505 510 Leu Arg Asn Asn Ser Leu Gln Thr PheSer Pro Gln Pro Gly Leu Glu 515 520 525 Arg Leu Trp Leu Asp Ala Asn ProTrp Asp Cys Ser Cys Pro Leu Lys 530 535 540 Ala Leu Arg Asp Phe Ala LeuGln Asn Pro Gly Val Val Pro Arg Phe 545 550 555 560 Val Gln Thr Val CysGlu Gly Asp Asp Cys Gln Pro Val Tyr Thr Tyr 565 570 575 Asn Asn Ile ThrCys Ala Gly Pro Ala Asn Val Ser Gly Leu Asp Leu 580 585 590 Arg Asp ValSer Glu Thr His Phe Val His Cys 595 600 (2) INFORMATION FOR SEQ IDNO:51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 409 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: LIS1 (human), Fig. 34 (xi) SEQUENCE DESCRIPTION: SEQID NO:51: Met Val Leu Ser Gln Arg Gln Arg Asp Glu Leu Asn Arg Ala IleAla 1 5 10 15 Asp Tyr Leu Arg Ser Asn Gly Tyr Glu Glu Ala Tyr Ser ValPhe Lys 20 25 30 Lys Glu Ala Glu Leu Asp Val Asn Glu Glu Leu Asp Lys LysTyr Ala 35 40 45 Gly Leu Leu Glu Lys Lys Trp Thr Ser Val Ile Arg Leu GlnLys Lys 50 55 60 Val Met Glu Leu Glu Ser Lys Leu Asn Glu Ala Lys Glu GluPhe Thr 65 70 75 80 Ser Gly Gly Pro Leu Gly Gln Lys Arg Asp Pro Lys GluTrp Ile Pro 85 90 95 Arg Pro Pro Glu Lys Tyr Ala Leu Ser Gly His Arg SerPro Val Thr 100 105 110 Arg Val Ile Phe His Pro Val Phe Ser Val Met ValSer Ala Ser Glu 115 120 125 Asp Ala Thr Ile Lys Val Trp Asp Tyr Glu ThrGly Asp Phe Glu Arg 130 135 140 Thr Leu Lys Gly His Thr Asp Ser Val GlnAsp Ile Ser Phe Asp His 145 150 155 160 Ser Gly Lys Leu Leu Ala Ser CysSer Ala Asp Met Thr Ile Lys Leu 165 170 175 Trp Asp Phe Gln Gly Phe GluCys Ile Arg Thr Met His Gly His Asp 180 185 190 His Asn Val Ser Ser ValAla Ile Met Pro Asn Gly Asp His Ile Val 195 200 205 Ser Ala Ser Arg AspLys Thr Ile Lys Met Trp Glu Val Gln Thr Gly 210 215 220 Tyr Cys Val LysThr Phe Thr Gly His Arg Glu Trp Val Arg Met Val 225 230 235 240 Arg ProAsn Gln Asp Gly Thr Leu Ile Ala Ser Cys Ser Asn Asp Gln 245 250 255 ThrVal Arg Val Trp Val Val Ala Thr Lys Glu Cys Lys Ala Glu Leu 260 265 270Arg Glu His Glu His Val Val Glu Cys Ile Ser Trp Ala Pro Glu Ser 275 280285 Ser Tyr Ser Ser Ile Ser Glu Ala Thr Gly Ser Glu Thr Lys Lys Ser 290295 300 Gly Lys Pro Gly Pro Phe Leu Leu Ser Gly Ser Arg Asp Lys Thr Lys305 310 315 320 Met Trp Asp Val Ser Thr Gly Met Cys Leu Met Thr Leu ValGly His 325 330 335 Asp Asn Trp Val Arg Gly Val Leu Phe His Ser Gly GlyLys Phe Ile 340 345 350 Leu Ser Cys Ala Asp Asp Lys Thr Leu Arg Val TrpAsp Tyr Lys Asn 355 360 365 Lys Arg Cys Met Lys Thr Leu Asn Ala His GluHis Phe Val Thr Ser 370 375 380 Leu Asp Phe His Lys Thr Ala Pro Tyr ValVal Thr Gly Ser Val Asp 385 390 395 400 Gln Thr Val Lys Val Trp Glu CysArg 405 (2) INFORMATION FOR SEQ ID NO:52: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 422 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: MD6, Fig. 35 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:52: Met Glu Arg Lys Asp Phe Glu Thr Trp Leu AspAsn Ile Ser Val Thr 1 5 10 15 Phe Leu Ser Leu Met Asp Leu Gln Lys AsnGlu Thr Leu Asp His Leu 20 25 30 Ile Ser Leu Ser Gly Ala Val Gln Leu ArgHis Leu Ser Asn Asn Leu 35 40 45 Glu Thr Leu Leu Lys Arg Asp Phe Leu LysLeu Leu Pro Leu Glu Leu 50 55 60 Ser Phe Tyr Leu Leu Lys Trp Leu Asp ProGln Thr Leu Leu Thr Cys 65 70 75 80 Cys Leu Val Ser Lys Gln Arg Asn LysVal Ile Ser Ala Cys Thr Glu 85 90 95 Val Trp Gln Thr Ala Cys Lys Asn LeuGly Trp Gln Ile Asp Asp Ser 100 105 110 Val Gln Asp Ser Leu His Trp LysLys Val Tyr Leu Lys Ala Ile Leu 115 120 125 Arg Met Lys Gln Leu Glu AspHis Glu Ala Phe Glu Thr Ser Ser Leu 130 135 140 Ile Gly His Ser Ala ArgVal Tyr Ala Leu Tyr Tyr Lys Asp Gly Leu 145 150 155 160 Leu Cys Thr GlySer Asp Asp Leu Ser Ala Lys Leu Trp Asp Val Ser 165 170 175 Thr Gly GlnCys Val Tyr Gly Ile Gln Thr His Thr Cys Ala Ala Val 180 185 190 Lys PheAsp Glu Gln Lys Leu Val Thr Gly Ser Phe Asp Asn Thr Val 195 200 205 AlaCys Trp Glu Trp Ser Ser Gly Ala Arg Thr Gln His Phe Arg Gly 210 215 220His Thr Gly Ala Val Phe Ser Val Asp Tyr Ser Asp Glu Leu Asp Ile 225 230235 240 Leu Val Ser Gly Ser Ala Asp Phe Ala Val Lys Val Trp Ala Leu Ser245 250 255 Ala Gly Thr Cys Leu Asn Thr Leu Thr Gly His Thr Glu Trp ValThr 260 265 270 Lys Val Val Leu Gln Lys Cys Lys Val Lys Ser Leu Leu HisSer Pro 275 280 285 Gly Asp Tyr Ile Leu Leu Ser Ala Asp Lys Tyr Glu IleLys Ile Trp 290 295 300 Pro Ile Gly Arg Glu Ile Asn Cys Lys Cys Leu LysThr Leu Ser Val 305 310 315 320 Ser Glu Asp Arg Ser Ile Cys Leu Gln ProArg Leu His Phe Asp Gly 325 330 335 Lys Tyr Ile Val Cys Ser Ser Ala LeuGly Leu Tyr Gln Trp Asp Phe 340 345 350 Ala Ser Tyr Asp Ile Leu Arg ValIle Lys Thr Pro Glu Val Ala Asn 355 360 365 Leu Ala Leu Leu Gly Phe GlyAsp Val Phe Ala Leu Leu Phe Asp Asn 370 375 380 His Tyr Leu Tyr Ile MetAsp Leu Arg Thr Glu Ser Leu Ile Ser Arg 385 390 395 400 Trp Pro Leu ProGlu Tyr Arg Lys Ser Lys Arg Gly Thr Ser Phe Leu 405 410 415 Ala Gly GluArg Pro Gly 420 (2) INFORMATION FOR SEQ ID NO:53: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 422 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: MSL1,Fig. 36 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53: Met Asn Gln Cys Ala LysAsp Ile Thr His Glu Ala Ser Ser Ile Pro 1 5 10 15 Ile Asp Leu Gln GluArg Tyr Ser His Trp Lys Lys Asn Thr Lys Leu 20 25 30 Leu Tyr Asp Tyr LeuAsn Thr Asn Ser Thr Lys Trp Pro Ser Leu Thr 35 40 45 Cys Gln Phe Phe ProAsp Leu Asp Thr Thr Ser Asp Glu His Arg Ile 50 55 60 Leu Leu Ser Ser PheThr Ser Ser Gln Lys Pro Glu Asp Glu Thr Ile 65 70 75 80 Tyr Ile Ser LysIle Ser Thr Leu Gly His Ile Lys Trp Ser Ser Leu 85 90 95 Asn Asn Phe AspMet Asp Glu Met Glu Phe Lys Pro Glu Asn Ser Thr 100 105 110 Arg Phe ProSer Lys His Leu Val Asn Asp Ile Ser Ile Phe Phe Pro 115 120 125 Asn GlyGlu Cys Asn Arg Ala Arg Tyr Leu Pro Gln Asn Pro Asp Ile 130 135 140 IleAla Gly Ala Ser Ser Asp Gly Ala Ile Tyr Ile Phe Asp Arg Thr 145 150 155160 Lys His Gly Ser Thr Arg Ile Arg Gln Ser Lys Ile Ser His Pro Phe 165170 175 Glu Thr Lys Leu Phe Gly Ser His Gly Val Ile Gln Asp Val Glu Ala180 185 190 Met Asp Thr Ser Ser Ala Asp Ile Asn Glu Ala Thr Ser Leu AlaTrp 195 200 205 Asn Leu Gln Gln Glu Ala Leu Leu Leu Ser Ser His Ser AsnGly Gln 210 215 220 Val Gln Val Trp Asp Ile Lys Gln Tyr Ser His Glu AsnPro Ile Ile 225 230 235 240 Asp Leu Pro Leu Val Ser Ile Asn Ser Asp GlyThr Ala Val Asn Asp 245 250 255 Val Thr Trp Met Pro Thr His Asp Ser LeuPhe Ala Ala Cys Thr Glu 260 265 270 Gly Asn Ala Val Ser Leu Leu Asp LeuArg Thr Lys Lys Glu Lys Leu 275 280 285 Gln Ser Asn Arg Glu Lys His AspGly Gly Val Asn Ser Cys Arg Phe 290 295 300 Asn Tyr Lys Asn Ser Leu IleLeu Ala Ser Ala Asp Ser Asn Gly Arg 305 310 315 320 Leu Asn Leu Trp AspIle Arg Asn Met Asn Lys Ser Pro Ile Ala Thr 325 330 335 Met Glu His GlyThr Ser Val Ser Thr Leu Glu Trp Ser Pro Asn Phe 340 345 350 Asp Thr ValLeu Ala Thr Ala Gly Gln Glu Asp Gly Leu Val Lys Leu 355 360 365 Trp AspThr Ser Cys Glu Glu Thr Ile Phe Thr His Gly Gly His Met 370 375 380 LeuGly Val Asn Asp Ile Ser Trp Asp Ala His Asp Pro Trp Leu Met 385 390 395400 Cys Ser Val Ala Asn Asp Asn Ser Val His Ile Trp Lys Pro Ala Gly 405410 415 Asn Leu Val Gly His Ser 420 (2) INFORMATION FOR SEQ ID NO:54:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 816 amino acids (B) TYPE:amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: MUS MUSCULUS PROTEIN, Fig. 37 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:54: Phe Arg Met Asp Asn Ala Ser Thr Arg Ile AspGlu Arg Phe Arg Ile 1 5 10 15 Asp Ala Tyr Ala Asn Ala Arg Tyr Pro MetPro Arg Thr Glu Ile Asn 20 25 30 Ser Glu Gln Glu Asn Cys Glu Asn Thr IleThr Leu Glu Asp Ser Glu 35 40 45 Gln Glu Asn Cys Glu Ala Ala Cys Met ProLeu Glu Thr Glu Ser Glu 50 55 60 Gln Glu Asn Cys Glu Met Ser Ser His GluSer Tyr Thr Asn Ala Ala 65 70 75 80 Glu Thr Pro Glu Asn Ile Ser Ile LeuSer Cys Leu Gly Glu Thr Ser 85 90 95 Gly Ala Leu Val Asp Thr Lys Thr IleSer Asp Ile Lys Thr Met Asp 100 105 110 Pro Arg Val Ser Leu Thr Pro SerSer Asp Val Thr Gly Thr Glu Asp 115 120 125 Ser Ser Val Leu Thr Pro GlnSer Thr Asp Val Asn Ser Val Asp Ser 130 135 140 Tyr Gln Gly Tyr Glu GlyAsp Asp Asp Asp Glu Glu Asp Asp Glu Asp 145 150 155 160 Asp Lys Asp GlyAsp Ser Asn Leu Pro Ser Leu Glu Asp Ser Asp Asn 165 170 175 Phe Ile SerCys Leu Glu Asn Ser Tyr Ile Pro Gln Asn Val Glu Asn 180 185 190 Gly GluVal Val Glu Glu Gln Ser Leu Gly Arg Arg Phe His Pro Tyr 195 200 205 GluLeu Glu Ala Gly Glu Val Val Glu Gly Gln Gly Gly Gly Ser Leu 210 215 220Phe Tyr Pro Tyr Glu Leu Glu Ala Gly Glu Val Val Glu Ala Gln Asn 225 230235 240 Val Gln Asn Leu Phe His Arg Tyr Glu Leu Glu Glu Gly Glu Val Val245 250 255 Glu Ala Gln Val Val Gln Ser Met Phe Pro Tyr Tyr Glu Leu GluAla 260 265 270 Gly Glu Val Val Glu Ala Glu Glu Val Gln Gly Phe Phe GlnArg Tyr 275 280 285 Glu Leu Glu Ala Arg Glu Val Ile Gly Ala Gln Gly GlyGln Gly Leu 290 295 300 Ser Arg His Tyr Gly Leu Glu Gly Gly Glu Val ValGlu Ala Thr Ala 305 310 315 320 Val Arg Arg Leu Ile Gln His His Glu LeuGlu Glu Gly Glu Asp Val 325 330 335 Asp Asp Gln Glu Glu Ser Ser Glu MetHis Glu Glu Thr Ser Glu Asp 340 345 350 Ser Ser Glu Gln Tyr Asp Ile GluAsp Asp Ser Leu Ile Asp Glu Trp 355 360 365 Ile Ala Leu Glu Thr Ser ProLeu Pro Arg Pro Arg Trp Asn Val Leu 370 375 380 Ser Ala Leu Arg Asp ArgGln Leu Gly Ser Ser Gly Arg Phe Val Tyr 385 390 395 400 Glu Ala Cys GlyAla Arg Leu Phe Val Gln Arg Phe Ser Leu Glu His 405 410 415 Val Phe GluGly His Ser Gly Cys Val Asn Thr Val His Phe Asn Gln 420 425 430 His GlyThr Leu Leu Ala Ser Gly Ser Asp Asp Leu Lys Val Ile Val 435 440 445 TrpAsp Trp Leu Lys Lys Arg Ser Val Leu Asn Phe Asp Ser Gly His 450 455 460Lys Asn Asn Ile Leu Gln Ala Lys Phe Leu Pro Asn Cys Asn Asp Ala 465 470475 480 Ile Leu Ala Met Cys Gly Arg Asp Gly Gln Val Arg Val Ala Gln Leu485 490 495 Ser Ala Val Ala Gly Thr His Met Thr Lys Arg Leu Val Lys HisGly 500 505 510 Gly Ala Ser His Arg Leu Gly Leu Glu Pro Asp Ser Pro PheArg Phe 515 520 525 Leu Thr Ser Gly Glu Asp Ala Val Val Phe Asn Ile AspLeu Arg Gln 530 535 540 Ala His Pro Ala Ser Lys Leu Leu Val Ile Lys AspGly Asp Lys Lys 545 550 555 560 Val Gly Leu Tyr Thr Val Phe Val Asn ProAla Asn Val Tyr Gln Phe 565 570 575 Ala Val Gly Gly Gln Asp Gln Phe MetArg Ile Tyr Asp Gln Arg Lys 580 585 590 Ile Asp Glu Asn Val Asn Asn GlyVal Leu Lys Lys Phe Cys Pro His 595 600 605 His Leu Leu Ser Ser Asp TyrPro Ala His Ile Thr Ser Leu Met Tyr 610 615 620 Ser Tyr Asp Gly Thr GluIle Leu Ala Ser Tyr Asn Asp Glu Asp Ile 625 630 635 640 Tyr Ile Phe AsnSer Ser Asp Ser Asp Gly Ala Gln Tyr Ala Lys Arg 645 650 655 Tyr Lys GlyHis Arg Asn Asn Ser Thr Val Lys Gly Val Tyr Phe Tyr 660 665 670 Gly ProArg Ser Glu Phe Val Met Ser Gly Ser Asp Cys Gly His Ile 675 680 685 PheIle Trp Glu Lys Ser Ser Cys Gln Ile Val Gln Phe Leu Glu Ala 690 695 700Asp Glu Gly Gly Thr Ile Asn Cys Ile Asp Ser His Pro Tyr Leu Pro 705 710715 720 Val Leu Ala Ser Ser Gly Leu Asp His Glu Val Lys Ile Trp Ser Pro725 730 735 Ile Ala Glu Pro Ser Lys Lys Leu Ala Gly Leu Lys Asn Val IleLys 740 745 750 Ile Asn Lys Leu Lys Arg Asp Asn Phe Thr Leu Arg His ThrSer Leu 755 760 765 Phe Asn Asn Ser Met Leu Cys Phe Leu Met Ser His ValThr Gln Ser 770 775 780 Asn Tyr Gly Arg Ser Trp Arg Gly Ile Arg Ile AsnAla Gly Gly Gly 785 790 795 800 Asp Phe Ser Asp Ser Ser Ser Ser Ser GluGlu Thr Asn Gln Glu Ser 805 810 815 (2) INFORMATION FOR SEQ ID NO:55:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 422 amino acids (B) TYPE:amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: ORF RB1, Fig. 38 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:55: Met Asn Gln Cys Ala Lys Asp Ile Thr His Glu Ala Ser Ser Ile Pro 15 10 15 Ile Asp Leu Gln Glu Arg Tyr Ser His Trp Lys Lys Asn Thr Lys Leu20 25 30 Leu Tyr Asp Tyr Leu Asn Thr Asn Ser Thr Lys Trp Pro Ser Leu Thr35 40 45 Cys Gln Phe Phe Pro Asp Leu Asp Thr Thr Ser Asp Glu His Arg Ile50 55 60 Leu Leu Ser Ser Phe Thr Ser Ser Gln Lys Pro Glu Asp Glu Thr Ile65 70 75 80 Tyr Ile Ser Lys Ile Ser Thr Leu Gly His Ile Lys Trp Ser SerLeu 85 90 95 Asn Asn Phe Asp Met Asp Glu Met Glu Phe Lys Pro Glu Asn SerThr 100 105 110 Arg Phe Pro Ser Lys His Leu Val Asn Asp Ile Ser Ile PhePhe Pro 115 120 125 Asn Gly Glu Cys Asn Arg Ala Arg Tyr Leu Pro Gln AsnPro Asp Ile 130 135 140 Ile Ala Gly Ala Ser Ser Asp Gly Ala Ile Tyr IlePhe Asp Arg Thr 145 150 155 160 Lys His Gly Ser Thr Arg Ile Arg Gln SerLys Ile Ser His Pro Phe 165 170 175 Glu Thr Lys Leu Phe Gly Ser His GlyVal Ile Gln Asp Val Glu Ala 180 185 190 Met Asp Thr Ser Ser Ala Asp IleAsn Glu Ala Thr Ser Leu Ala Trp 195 200 205 Asn Leu Gln Gln Glu Ala LeuLeu Leu Ser Ser His Ser Asn Gly Gln 210 215 220 Val Gln Val Trp Asp IleLys Gln Tyr Ser His Glu Asn Pro Ile Ile 225 230 235 240 Asp Leu Pro LeuVal Ser Ile Asn Ser Asp Gly Thr Ala Val Asn Asp 245 250 255 Val Thr TrpMet Pro Thr His Asp Ser Leu Phe Ala Ala Cys Thr Glu 260 265 270 Gly AsnAla Val Ser Leu Leu Asp Leu Arg Thr Lys Lys Glu Lys Leu 275 280 285 GlnSer Asn Arg Glu Lys His Asp Gly Gly Val Asn Ser Cys Arg Phe 290 295 300Asn Tyr Lys Asn Ser Leu Ile Leu Ala Ser Ala Asp Ser Asn Gly Arg 305 310315 320 Leu Asn Leu Trp Asp Ile Arg Asn Met Asn Lys Ser Pro Ile Ala Thr325 330 335 Met Glu His Gly Thr Ser Val Ser Thr Leu Glu Trp Ser Pro AsnPhe 340 345 350 Asp Thr Val Leu Ala Thr Ala Gly Gln Glu Asp Gly Leu ValLys Leu 355 360 365 Trp Asp Thr Ser Cys Glu Glu Thr Ile Phe Thr His GlyGly His Met 370 375 380 Leu Gly Val Asn Asp Ile Ser Trp Asp Ala His AspPro Trp Leu Met 385 390 395 400 Cys Ser Val Ala Asn Asp Asn Ser Val HisIle Trp Lys Pro Ala Gly 405 410 415 Asn Leu Val Gly His Ser 420 (2)INFORMATION FOR SEQ ID NO:56: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:576 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: Periodic Trp protein, Fig. 39 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:56: Met Ile Ser Ala Thr Asn Trp Val ProArg Gly Phe Ser Ser Glu Phe 1 5 10 15 Pro Glu Lys Tyr Val Leu Asp AspGlu Glu Val Glu Arg Ile Asn Gln 20 25 30 Leu Ala Gln Leu Asn Leu Asp AspAla Lys Ala Thr Leu Glu Glu Ala 35 40 45 Glu Gly Glu Ser Gly Val Glu AspAsp Ala Ala Thr Gly Ser Ser Asn 50 55 60 Lys Leu Lys Asp Gln Leu Asp IleAsp Asp Asp Leu Lys Glu Tyr Asn 65 70 75 80 Leu Glu Glu Tyr Asp Asp GluGlu Ile Ala Asp Asn Glu Gly Gly Lys 85 90 95 Asp Val Ser Met Phe Pro GlyLeu Ser Asn Asp Ser Asp Val Lys Phe 100 105 110 His Glu Gly Glu Lys GlyGlu Asp Pro Tyr Ile Ser Leu Pro Asn Gln 115 120 125 Glu Asp Ser Gln GluGlu Lys Gln Glu Leu Gln Val Tyr Pro Ser Asp 130 135 140 Asn Leu Val LeuAla Ala Arg Thr Glu Asp Asp Val Ser Tyr Leu Asp 145 150 155 160 Ile TyrVal Tyr Asp Asp Gly Ala Gly Phe His Ser Ser Asp Ile Pro 165 170 175 ValGlu Glu Gly Asp Glu Ala Asp Pro Asp Val Ala Arg Gly Leu Val 180 185 190Arg Asp Pro Ala Leu Tyr Val His His Asp Leu Met Leu Pro Ala Phe 195 200205 Pro Leu Cys Val Glu Trp Leu Asp Tyr Lys Val Gly Ser Asn Ser Glu 210215 220 Glu Ala Ala Asn Tyr Ala Ala Ile Gly Thr Phe Asp Pro Gln Ile Glu225 230 235 240 Ile Trp Asn Leu Asp Cys Val Asp Lys Ala Phe Pro Asp MetIle Leu 245 250 255 Gly Glu Pro Leu Asp Asn Ser Met Val Ser Leu Lys SerLys Lys Lys 260 265 270 Lys Lys Lys Ser Lys Thr Gly His Ile Thr Thr HisHis Thr Asp Ala 275 280 285 Val Leu Ser Met Ala His Asn Lys Tyr Phe ArgSer Val Leu Ala Ser 290 295 300 Thr Ser Ala Asp His Thr Val Lys Leu TrpAsp Leu Asn Ser Gly Asn 305 310 315 320 Ala Ala Arg Ser Leu Ala Ser IleHis Ser Asn Lys Asn Val Ser Ser 325 330 335 Ser Glu Trp His Met Leu AsnGly Ser Ile Leu Leu Thr Gly Gly Tyr 340 345 350 Asp Ser Arg Val Ala LeuThr Asp Val Arg Ile Ser Asp Glu Ser Gln 355 360 365 Met Ser Lys Tyr TrpSer Ala Met Ala Gly Glu Glu Ile Glu Thr Val 370 375 380 Thr Phe Ala SerGlu Asn Ile Ile Leu Cys Gly Thr Asp Ser Gly Asn 385 390 395 400 Val TyrSer Phe Asp Ile Arg Asn Asn Glu Asn Arg Lys Pro Val Trp 405 410 415 ThrLeu Lys Ala His Asp Ala Gly Ile Ser Thr Leu Cys Ser Asn Lys 420 425 430Phe Ile Pro Gly Met Met Ser Thr Gly Ala Met Gly Glu Lys Thr Val 435 440445 Lys Leu Trp Lys Phe Pro Leu Asp Asp Ala Thr Asn Thr Lys Gly Pro 450455 460 Ser Met Val Leu Ser Arg Asp Phe Asp Val Gly Asn Val Leu Thr Ser465 470 475 480 Ser Phe Ala Pro Asp Ile Glu Val Ala Gly Thr Met Val IleGly Gly 485 490 495 Val Asn Lys Val Leu Lys Leu Trp Asp Val Phe Thr AsnArg Ser Val 500 505 510 Arg Lys Ser Phe Lys Ser Glu Leu Glu Asn Val GlnAla Arg Ala Lys 515 520 525 Glu Glu Ala Gln Lys Ile Gly Lys Ser Ser ArgIle Ala Arg Lys Tyr 530 535 540 Thr Ser Asn Asp Asn Pro Asp Thr Val IleThr Ile Asp Asp Gln Gly 545 550 555 560 Glu Asp Glu Glu Glu Arg Glu GlyGly Asp Glu His Asp Asp Met Ala 565 570 575 (2) INFORMATION FOR SEQ IDNO:57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 325 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: PLAP, Fig. 40 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:57: Met His Tyr Met Ser Gly His Ser Asn Phe Val Ser Tyr Val Cys Ile 15 10 15 Ile Pro Ser Ser Asp Ile Tyr Pro His Gly Leu Ile Ala Thr Gly Gly20 25 30 Asn Asp His Asn Ile Cys Ile Phe Ser Leu Asp Ser Pro Met Pro Leu35 40 45 Tyr Ile Leu Lys Gly His Lys Asp Thr Val Cys Ser Leu Ser Ser Gly50 55 60 Lys Phe Gly Thr Leu Leu Ser Gly Ser Trp Asp Thr Thr Ala Lys Val65 70 75 80 Trp Leu Asn Asp Lys Cys Met Met Thr Leu Gln Gly His Thr AlaAla 85 90 95 Val Trp Ala Val Lys Ile Leu Pro Glu Gln Gly Leu Met Leu ThrGly 100 105 110 Ser Ala Asp Lys Thr Ile Lys Leu Trp Lys Ala Gly Arg CysGlu Arg 115 120 125 Thr Phe Leu Gly His Glu Asp Cys Val Arg Gly Leu AlaIle Leu Ser 130 135 140 Glu Thr Glu Phe Leu Ser Cys Ala Asn Asp Ala SerIle Arg Arg Trp 145 150 155 160 Gln Ile Thr Gly Glu Cys Leu Glu Val TyrPhe Gly His Thr Asn Tyr 165 170 175 Ile Tyr Ser Ile Ser Val Phe Pro AsnSer Lys Asp Phe Val Thr Thr 180 185 190 Ala Glu Asp Arg Ser Leu Arg IleTrp Lys His Gly Glu Cys Ala Gln 195 200 205 Thr Ile Arg Leu Pro Ala GlnSer Ile Trp Cys Cys Cys Val Leu Glu 210 215 220 Asn Gly Asp Ile Val ValGly Ala Ser Asp Gly Ile Ile Arg Val Phe 225 230 235 240 Thr Glu Ser GluGlu Arg Thr Ala Ser Ala Glu Glu Ile Lys Ala Ser 245 250 255 Leu Ser ArgGlu Ser Pro Leu Ile Ala Lys Val Leu Thr Thr Glu Pro 260 265 270 Pro IleIle Thr Pro Val Arg Arg Thr Leu Pro Cys Arg Val Thr Arg 275 280 285 SerMet Ile Ser Ser Cys Leu Ser Arg Leu Val Ser Thr Ser Leu Ser 290 295 300Thr Ser Asp Ser His Leu Thr Ile Thr Ala Leu His Leu Phe Leu Thr 305 310315 320 Thr Thr Thr Thr Glu 325 (2) INFORMATION FOR SEQ ID NO:58: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 425 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDING PROTEIN - HUMAN, Fig. 41 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:58: Met Ala Asp Lys Glu Ala Ala Phe AspAsp Ala Val Glu Glu Arg Val 1 5 10 15 Ile Asn Glu Glu Tyr Lys Ile TrpLys Lys Asn Thr Pro Phe Leu Tyr 20 25 30 Asp Leu Val Met Thr His Ala LeuGlu Trp Pro Ser Leu Thr Ala Gln 35 40 45 Trp Leu Pro Asp Val Thr Arg ProGlu Gly Lys Asp Phe Ser Ile His 50 55 60 Arg Leu Val Leu Gly Thr His ThrSer Asp Glu Gln Asn His Leu Val 65 70 75 80 Ile Ala Ser Val Gln Leu ProAsn Asp Asp Ala Gln Phe Asp Ala Ser 85 90 95 His Tyr Asp Ser Glu Lys GlyGlu Phe Gly Gly Phe Gly Ser Val Ser 100 105 110 Gly Lys Ile Glu Ile GluIle Lys Ile Asn His Glu Gly Glu Val Asn 115 120 125 Arg Ala Arg Tyr MetPro Gln Asn Pro Cys Ile Ile Ala Thr Lys Thr 130 135 140 Pro Ser Ser AspVal Leu Val Phe Asp Tyr Thr Lys His Pro Ser Lys 145 150 155 160 Pro AspPro Ser Gly Glu Cys Asn Pro Asp Leu Arg Leu Arg Gly His 165 170 175 GlnLys Glu Gly Tyr Gly Leu Ser Trp Asn Pro Asn Leu Ser Gly His 180 185 190Leu Leu Ser Ala Ser Asp Asp His Thr Ile Cys Leu Trp Asp Ile Ser 195 200205 Ala Val Pro Lys Glu Gly Lys Val Val Asp Ala Lys Thr Ile Phe Thr 210215 220 Gly His Thr Ala Val Val Glu Asp Val Ser Trp His Leu Leu His Glu225 230 235 240 Ser Leu Phe Gly Ser Val Ala Asp Asp Gln Lys Leu Met IleTrp Asp 245 250 255 Thr Arg Ser Asn Asn Thr Ser Lys Pro Ser His Ser ValAsp Ala His 260 265 270 Thr Ala Glu Val Asn Cys Leu Ser Phe Asn Pro TyrSer Glu Phe Ile 275 280 285 Leu Ala Thr Gly Ser Ala Asp Lys Thr Val AlaLeu Trp Asp Leu Arg 290 295 300 Asn Leu Lys Leu Lys Leu His Ser Phe GluSer His Lys Asp Glu Ile 305 310 315 320 Phe Gln Val Gln Trp Ser Pro HisAsn Glu Thr Ile Leu Ala Ser Ser 325 330 335 Gly Thr Asp Arg Arg Leu AsnVal Trp Asp Leu Ser Lys Ile Gly Glu 340 345 350 Glu Gln Ser Pro Glu AspAla Glu Asp Gly Pro Pro Glu Leu Leu Phe 355 360 365 Ile His Gly Gly HisThr Ala Lys Ile Ser Asp Phe Ser Trp Asn Pro 370 375 380 Asn Glu Pro TrpVal Ile Cys Ser Val Ser Glu Asp Asn Ile Met Gln 385 390 395 400 Val TrpGln Met Ala Glu Asn Ile Tyr Asn Asp Glu Asp Pro Glu Gly 405 410 415 SerVal Asp Pro Glu Gly Gln Gly Ser 420 425 (2) INFORMATION FOR SEQ IDNO:59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 852 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: S253 PROTEIN, Fig. 42 (xi) SEQUENCE DESCRIPTION: SEQID NO:59: Met Phe Lys Ser Lys Thr Ser Thr Leu Ser Tyr Asp Glu Thr ProAsn 1 5 10 15 Ser Asn Glu Gly Asp Arg Asn Ala Thr Pro Val Asn Pro LysGlu Lys 20 25 30 Ser Gln Thr Lys His Leu Asn Ile Pro Gly Asp Arg Ser ArgHis Ser 35 40 45 Ser Ile Ala Asp Ser Lys Arg Ser Ser Ser Arg Tyr Asp GlyGly Tyr 50 55 60 Ser Ala Asp Ile Ile Pro Ala Gln Leu Arg Phe Ile Asp AsnIle Asp 65 70 75 80 Tyr Gly Thr Arg Leu Arg Lys Thr Leu His Arg Asn SerVal Val Ser 85 90 95 Asn Gly Tyr Asn Lys Leu Ser Glu Asn Asp Arg Trp TyrPhe Asp Leu 100 105 110 Phe Asp Arg Lys Tyr Phe Glu Asn Tyr Leu Glu GluPro Thr Tyr Ile 115 120 125 Lys Ile Phe Lys Lys Lys Glu Gly Leu Glu GlnPhe Asp Arg Met Phe 130 135 140 Leu Ala Gln Glu Leu Lys Ile Pro Asp ValTyr Lys Ser Thr Thr Tyr 145 150 155 160 Gln Gly Glu Pro Ala Val Ala AsnSer Glu Leu Phe Lys Asn Ser Ile 165 170 175 Cys Cys Cys Thr Phe Ser HisAsp Gly Lys Tyr Met Val Ile Gly Cys 180 185 190 Lys Asp Gly Ser Leu HisLeu Trp Lys Val Ile Asn Ser Pro Val Lys 195 200 205 Arg Ser Glu Met GlyArg Ser Glu Lys Ser Val Ser Ala Ser Arg Ala 210 215 220 Asn Ser Leu LysIle Gln Arg His Leu Ala Ser Ile Ser Ser His Asn 225 230 235 240 Gly SerIle Ser Ser Asn Asp Leu Lys Pro Ser Asp Gln Phe Glu Gly 245 250 255 ProSer Lys Gln Leu His Leu Tyr Ala Pro Val Phe Tyr Ser Asp Val 260 265 270Phe Arg Val Phe Met Glu His Ala Leu Asp Ile Leu Asp Ala Asn Trp 275 280285 Ser Lys Asn Gly Phe Leu Ile Thr Ala Ser Met Asp Lys Thr Ala Lys 290295 300 Leu Trp His Pro Glu Arg Lys Tyr Ser Leu Lys Thr Phe Val His Pro305 310 315 320 Asp Phe Val Thr Ser Ala Ile Phe Phe Pro Asn Asp Asp ArgPhe Ile 325 330 335 Ile Thr Gly Cys Leu Asp His Arg Cys Arg Leu Trp SerIle Leu Asp 340 345 350 Asn Glu Val Ser Tyr Ala Phe Asp Cys Lys Asp LeuIle Thr Ser Leu 355 360 365 Thr Leu Ser Pro Pro Gly Gly Glu Tyr Thr IleIle Gly Thr Phe Asn 370 375 380 Gly Tyr Ile Tyr Val Leu Leu Thr His GlyLeu Lys Phe Val Ser Ser 385 390 395 400 Phe His Val Ser Asp Lys Ser ThrGln Gly Thr Thr Lys Asn Ser Phe 405 410 415 His Pro Ser Ser Glu Tyr GlyLys Val Gln His Gly Pro Arg Ile Thr 420 425 430 Gly Leu Gln Cys Phe PheSer Lys Val Asp Lys Asn Leu Arg Leu Ile 435 440 445 Val Thr Thr Asn AspSer Lys Ile Gln Ile Phe Asp Leu Asn Glu Lys 450 455 460 Lys Pro Leu GluLeu Phe Lys Gly Phe Gln Ser Gly Ser Ser Arg His 465 470 475 480 Arg GlyGln Phe Leu Met Met Lys Asn Glu Pro Val Val Phe Thr Gly 485 490 495 SerAsp Asp His Trp Phe Tyr Thr Trp Lys Met Gln Ser Phe Asn Leu 500 505 510Ser Ala Glu Met Asn Cys Thr Ala Pro His Arg Lys Lys Arg Leu Ser 515 520525 Gly Ser Met Ser Leu Lys Gly Leu Leu Arg Ile Val Ser Asn Lys Ser 530535 540 Thr Asn Asp Glu Cys Leu Thr Glu Thr Ser Asn Gln Ser Ser Ser His545 550 555 560 Thr Phe Thr Asn Ser Ser Lys Asn Val Leu Gln Thr Gln ThrVal Gly 565 570 575 Ser Gln Ala Ile Lys Asn Asn His Tyr Ile Ser Phe HisAla His Asn 580 585 590 Ser Pro Val Thr Cys Ala Ser Ile Ala Pro Asp ValAla Ile Lys Asn 595 600 605 Leu Ser Leu Ser Asn Asp Leu Ile Phe Glu LeuThr Ser Gln Tyr Phe 610 615 620 Lys Glu Met Gly Gln Asn Tyr Ser Glu SerLys Glu Thr Cys Asp Asn 625 630 635 640 Lys Pro Asn His Pro Val Thr GluThr Gly Gly Phe Ser Ser Asn Leu 645 650 655 Ser Asn Val Val Asn Asn ValGly Thr Ile Leu Ile Thr Thr Asp Ser 660 665 670 Gln Gly Leu Ile Arg ValPhe Arg Thr Asp Ile Leu Pro Glu Ile Arg 675 680 685 Lys Lys Ile Ile GluLys Phe His Glu Tyr Asn Leu Phe His Leu Glu 690 695 700 Ala Ala Gly LysIle Asn Asn His Asn Asn Asp Ser Ile Leu Glu Asn 705 710 715 720 Arg MetAsp Glu Arg Ser Ser Thr Glu Asp Asn Glu Phe Ser Thr Thr 725 730 735 ProPro Ser Asn Thr His Asn Ser Arg Pro Ser His Asp Phe Cys Glu 740 745 750Leu His Pro Asn Asn Ser Pro Val Ile Ser Gly Met Pro Ser Arg Ala 755 760765 Ser Ala Ile Phe Lys Asn Ser Ile Phe Asn Lys Ser Asn Gly Ser Phe 770775 780 Ile Ser Leu Lys Ser Arg Ser Glu Ser Thr Ser Ser Thr Val Phe Gly785 790 795 800 Pro His Asp Ile Pro Arg Val Ser Thr Thr Tyr Pro Lys LeuLys Cys 805 810 815 Asp Val Cys Asn Gly Ser Asn Phe Glu Cys Ala Ser LysAsn Pro Ile 820 825 830 Ala Gly Gly Asp Ser Gly Phe Thr Cys Ala Asp CysGly Thr Ile Leu 835 840 845 Asn Asn Phe Arg 850 (2) INFORMATION FOR SEQID NO:60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 488 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: SOF1, Fig. 43 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:60: Met Lys Ile Lys Thr Ile Lys Arg Ser Ala Asp Asp Tyr Val Pro Val 15 10 15 Lys Ser Thr Gln Glu Ser Gln Met Pro Arg Asn Leu Asn Pro Glu Leu20 25 30 His Pro Phe Glu Arg Ala Arg Glu Tyr Thr Lys Ala Leu Asn Ala Thr35 40 45 Lys Leu Glu Arg Met Phe Ala Lys Pro Phe Val Gly Gln Leu Gly Tyr50 55 60 Gly His Arg Asp Gly Val Tyr Ala Ile Ala Lys Asn Tyr Gly Ser Leu65 70 75 80 Asn Lys Leu Ala Thr Gly Ser Ala Asp Gly Val Ile Lys Tyr TrpAsn 85 90 95 Met Ser Thr Arg Glu Glu Phe Val Ser Phe Lys Ala His Tyr GlyLeu 100 105 110 Val Thr Gly Leu Cys Val Thr Gln Pro Arg Phe His Asp LysLys Pro 115 120 125 Asp Leu Lys Ser Gln Asn Phe Met Leu Ser Cys Ser AspAsp Lys Thr 130 135 140 Val Lys Leu Trp Ser Ile Asn Val Asp Asp Tyr SerAsn Lys Asn Ser 145 150 155 160 Ser Asp Asn Asp Ser Val Thr Asn Glu GluGly Leu Ile Arg Thr Phe 165 170 175 Asp Gly Glu Ser Ala Phe Gln Gly IleAsp Ser His Arg Glu Asn Ser 180 185 190 Thr Phe Ala Thr Gly Gly Ala LysIle His Leu Trp Asp Val Asn Arg 195 200 205 Leu Lys Pro Val Ser Asp LeuSer Trp Gly Ala Asp Asn Ile Thr Ser 210 215 220 Leu Lys Phe Asn Gln AsnGlu Thr Asp Ile Leu Ala Ser Thr Gly Ser 225 230 235 240 Asp Asn Ser IleVal Leu Tyr Asp Leu Arg Thr Asn Ser Pro Thr Gln 245 250 255 Lys Ile ValGln Thr Met Arg Thr Asn Ala Ile Cys Trp Asn Pro Met 260 265 270 Glu AlaPhe Asn Phe Val Thr Ala Asn Glu Asp His Asn Ala Tyr Tyr 275 280 285 TyrAsp Met Arg Asn Leu Ser Arg Ser Leu Asn Val Phe Lys Asp His 290 295 300Val Ser Ala Val Met Asp Val Asp Phe Ser Pro Thr Gly Asp Glu Ile 305 310315 320 Val Thr Gly Ser Tyr Asp Lys Ser Ile Arg Ile Tyr Lys Thr Asn His325 330 335 Gly His Ser Arg Glu Ile Tyr His Thr Lys Arg Met Gln His ValPhe 340 345 350 Val Lys Tyr Ser Met Asp Ser Lys Tyr Ile Ile Ser Gly SerAsp Asp 355 360 365 Gly Asn Val Arg Leu Trp Arg Ser Lys Ala Trp Glu ArgSer Asn Val 370 375 380 Lys Thr Thr Arg Glu Lys Asn Lys Leu Glu Tyr AspGlu Lys Leu Lys 385 390 395 400 Glu Arg Phe Arg His Met Pro Glu Ile LysArg Ile Ser Arg His Arg 405 410 415 His Val Pro Gln Val Ile Lys Lys AlaGln Glu Ile Lys Asn Ile Glu 420 425 430 Leu Ser Ser Ile Lys Arg Arg GluAla Asn Glu Arg Arg Thr Arg Lys 435 440 445 Asp Met Pro Tyr Ile Ser GluArg Lys Lys Gln Ile Val Gly Thr Val 450 455 460 His Lys Tyr Glu Asp SerGly Arg Asp Arg Lys Arg Arg Lys Glu Asp 465 470 475 480 Asp Lys Arg AspThr Gln Glu Lys 485 (2) INFORMATION FOR SEQ ID NO:61: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 423 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: STE4 -YEAST, Fig. 44 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:61: Met Ala Ala HisGln Met Asp Ser Ile Thr Tyr Ser Asn Asn Val Thr 1 5 10 15 Gln Gln TyrIle Gln Pro Gln Ser Leu Gln Asp Ile Ser Ala Val Glu 20 25 30 Asp Glu IleGln Asn Lys Ile Glu Ala Ala Arg Gln Glu Ser Lys Gln 35 40 45 Leu His AlaGln Ile Asn Lys Ala Lys His Lys Ile Gln Asp Ala Ser 50 55 60 Leu Phe GlnMet Ala Asn Lys Val Thr Ser Leu Thr Lys Asn Lys Ile 65 70 75 80 Asn LeuLys Pro Asn Ile Val Leu Lys Gly His Asn Asn Lys Ile Ser 85 90 95 Asp PheArg Trp Ser Arg Asp Ser Lys Arg Ile Leu Ser Ala Ser Gln 100 105 110 AspGly Phe Met Leu Ile Trp Asp Ser Ala Ser Gly Leu Lys Gln Asn 115 120 125Ala Ile Pro Leu Asp Ser Gln Trp Val Leu Ser Cys Ala Ile Ser Pro 130 135140 Ser Ser Thr Leu Val Ala Ser Ala Gly Leu Asn Asn Asn Cys Thr Ile 145150 155 160 Tyr Arg Val Ser Lys Glu Asn Arg Val Ala Gln Asn Val Ala SerIle 165 170 175 Phe Lys Gly His Thr Cys Tyr Ile Ser Asp Ile Glu Phe ThrAsp Asn 180 185 190 Ala His Ile Leu Thr Ala Ser Gly Asp Met Thr Cys AlaLeu Trp Asp 195 200 205 Ile Pro Lys Ala Lys Arg Val Arg Glu Tyr Ser AspHis Leu Gly Asp 210 215 220 Val Leu Ala Leu Ala Ile Pro Glu Glu Pro AsnLeu Glu Asn Ser Ser 225 230 235 240 Asn Thr Phe Ala Ser Cys Gly Ser AspGly Tyr Thr Tyr Ile Trp Asp 245 250 255 Ser Arg Ser Pro Ser Ala Val GlnSer Phe Tyr Val Asn Asp Ser Asp 260 265 270 Ile Asn Ala Leu Arg Phe PheLys Asp Gly Met Ser Ile Val Ala Gly 275 280 285 Ser Asp Asn Gly Ala IleAsn Met Tyr Asp Leu Arg Ser Asp Cys Ser 290 295 300 Ile Ala Thr Phe SerLeu Phe Arg Gly Tyr Glu Glu Arg Thr Pro Thr 305 310 315 320 Pro Thr TyrMet Ala Ala Asn Met Glu Tyr Asn Thr Ala Gln Ser Pro 325 330 335 Gln ThrLeu Lys Ser Thr Ser Ser Ser Tyr Leu Asp Asn Gln Gly Val 340 345 350 ValSer Leu Asp Phe Ser Ala Ser Gly Arg Leu Met Tyr Ser Cys Tyr 355 360 365Thr Asp Ile Gly Cys Val Val Trp Asp Val Leu Lys Gly Glu Ile Val 370 375380 Gly Lys Leu Glu Gly His Gly Gly Arg Val Thr Gly Val Arg Ser Ser 385390 395 400 Pro Asp Gly Leu Ala Val Cys Thr Gly Ser Trp Asp Ser Thr MetLys 405 410 415 Ile Trp Ser Pro Gly Tyr Gln 420 (2) INFORMATION FOR SEQID NO:62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 704 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TRANSCRIPTION FACTOR TIIF, Fig. 45 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:62: Met Ser Leu Glu Val Ser Asn Ile Asn Gly GlyAsn Gly Thr Gln Leu 1 5 10 15 Ser His Asp Lys Arg Glu Leu Leu Cys LeuLeu Lys Leu Ile Lys Lys 20 25 30 Tyr Gln Leu Lys Ser Thr Glu Glu Leu LeuCys Gln Glu Ala Asn Val 35 40 45 Ser Ser Val Glu Leu Ser Glu Ile Ser GluSer Asp Val Gln Gln Val 50 55 60 Leu Gly Ala Val Leu Gly Ala Gly Asp AlaAsn Arg Glu Arg Lys His 65 70 75 80 Val Gln Ser Pro Ala Gln Gly His LysGln Ser Ala Val Thr Glu Ala 85 90 95 Asn Ala Ala Glu Glu Leu Ala Lys PheIle Asp Asp Asp Ser Phe Asp 100 105 110 Ala Gln His Tyr Glu Gln Ala TyrLys Glu Leu Arg Thr Phe Val Glu 115 120 125 Asp Ser Leu Asp Ile Tyr LysHis Glu Leu Ser Met Val Leu Tyr Pro 130 135 140 Ile Leu Val Gln Ile TyrPhe Lys Ile Leu Ala Ser Gly Leu Arg Glu 145 150 155 160 Lys Ala Lys GluPhe Ile Glu Lys Tyr Lys Cys Asp Leu Asp Gly Tyr 165 170 175 Tyr Ile GluGly Leu Phe Asn Leu Leu Leu Leu Ser Lys Pro Glu Glu 180 185 190 Leu LeuGlu Asn Asp Leu Val Val Ala Met Glu Gln Asp Lys Phe Val 195 200 205 IleArg Met Ser Arg Asp Ser His Ser Leu Phe Lys Arg His Ile Gln 210 215 220Asp Arg Arg Gln Glu Val Val Ala Asp Ile Val Ser Lys Tyr Leu His 225 230235 240 Phe Asp Thr Tyr Glu Gly Met Ala Arg Asn Lys Leu Gln Cys Val Ala245 250 255 Thr Ala Gly Ser His Leu Gly Glu Ala Lys Arg Gln Asp Asn LysMet 260 265 270 Arg Val Tyr Tyr Gly Leu Leu Lys Glu Val Asp Phe Gln ThrLeu Thr 275 280 285 Thr Pro Ala Pro Ala Pro Glu Glu Glu Asp Asp Asp ProAsp Ala Pro 290 295 300 Asp Arg Pro Lys Lys Lys Lys Pro Lys Lys Asp ProLeu Leu Ser Lys 305 310 315 320 Lys Ser Lys Ser Asp Pro Asn Ala Pro SerIle Asp Arg Ile Pro Leu 325 330 335 Pro Glu Leu Lys Asp Ser Asp Lys LeuLeu Lys Leu Lys Ala Leu Arg 340 345 350 Glu Ala Ser Lys Arg Leu Ala LeuSer Lys Asp Gln Leu Pro Ser Ala 355 360 365 Val Phe Tyr Thr Val Leu AsnSer His Gln Gly Val Thr Cys Ala Glu 370 375 380 Ile Ser Asp Asp Ser ThrMet Leu Ala Cys Gly Phe Gly Asp Ser Ser 385 390 395 400 Val Arg Ile TrpSer Leu Thr Pro Ala Asn Val Arg Thr Leu Lys Asp 405 410 415 Ala Asp SerLeu Arg Glu Leu Asp Lys Glu Ser Ala Asp Ile Asn Val 420 425 430 Arg MetLeu Asp Asp Arg Ser Gly Glu Val Thr Arg Ser Leu Met Gly 435 440 445 HisThr Gly Pro Val Tyr Arg Cys Ala Phe Ala Pro Glu Met Asn Leu 450 455 460Leu Leu Ser Cys Ser Glu Asp Ser Thr Ile Arg Leu Trp Ser Leu Leu 465 470475 480 Thr Trp Ser Cys Val Val Thr Tyr Arg Gly His Val Tyr Pro Val Trp485 490 495 Asp Val Arg Phe Ala Pro His Gly Tyr Tyr Phe Val Ser Cys SerTyr 500 505 510 Asp Lys Thr Ala Arg Leu Trp Ala Thr Asp Ser Asn Gln AlaLeu Arg 515 520 525 Val Phe Val Gly His Leu Ser Asp Val Asp Cys Val GlnPhe His Pro 530 535 540 Asn Ser Asn Tyr Val Ala Thr Gly Ser Ser Asp ArgThr Val Arg Leu 545 550 555 560 Trp Asp Asn Met Thr Gly Gln Ser Val ArgLeu Met Thr Gly His Lys 565 570 575 Gly Ser Val Ser Ser Leu Ala Phe SerAla Cys Gly Arg Tyr Leu Ala 580 585 590 Ser Gly Ser Val Asp His Asn IleIle Ile Trp Asp Leu Ser Asn Gly 595 600 605 Ser Leu Val Thr Thr Leu LeuArg His Thr Ser Thr Val Thr Thr Ile 610 615 620 Thr Phe Ser Arg Asp GlyThr Val Leu Ala Ala Ala Gly Leu Asp Asn 625 630 635 640 Asn Leu Thr LeuTrp Asp Phe His Lys Val Thr Glu Asp Tyr Ile Ser 645 650 655 Asn His IleThr Val Ser His His Gln Asp Glu Asn Asp Glu Asp Val 660 665 670 Tyr LeuMet Arg Thr Phe Pro Ser Lys Asn Ser Pro Phe Val Ser Leu 675 680 685 HisPhe Thr Arg Arg Asn Leu Leu Met Cys Val Gly Leu Phe Lys Ser 690 695 700(2) INFORMATION FOR SEQ ID NO:63: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 713 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1, Fig. 46 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:63: Met Thr Ala Ser Val Ser Asn Thr Gln Asn LysLeu Asn Glu Leu Leu 1 5 10 15 Asp Ala Ile Arg Gln Glu Phe Leu Gln ValSer Gln Glu Ala Asn Thr 20 25 30 Tyr Arg Leu Gln Asn Gln Lys Asp Tyr AspPhe Lys Met Asn Gln Gln 35 40 45 Leu Ala Glu Met Gln Gln Ile Arg Asn ThrVal Tyr Glu Leu Glu Leu 50 55 60 Thr His Arg Lys Met Lys Asp Ala Tyr GluAla Glu Ile Lys His Leu 65 70 75 80 Lys Leu Gly Leu Glu Gln Arg Asp HisGln Ile Ala Ser Leu Thr Val 85 90 95 Gln Gln Gln Gln Gln Gln Gln Gln GlnGln Gln Val Gln Gln His Leu 100 105 110 Gln Gln Gln Gln Gln Gln Leu AlaAla Ala Ser Ala Ser Val Pro Val 115 120 125 Ala Gln Gln Pro Pro Ala ThrThr Ser Ala Thr Ala Thr Pro Ala Ala 130 135 140 Asn Thr Thr Thr Gly SerPro Ser Ala Phe Pro Val Gln Ala Ser Arg 145 150 155 160 Pro Asn Leu ValGly Ser Gln Leu Pro Thr Thr Thr Leu Pro Val Val 165 170 175 Ser Ser AsnAla Gln Gln Gln Leu Pro Gln Gln Gln Leu Gln Gln Gln 180 185 190 Gln LeuGln Gln Gln Gln Pro Pro Pro Gln Val Ser Val Ala Pro Leu 195 200 205 SerAsn Thr Ala Ile Asn Gly Ser Pro Thr Ser Lys Glu Thr Thr Thr 210 215 220Leu Pro Ser Val Lys Ala Pro Glu Ser Thr Leu Lys Glu Thr Glu Pro 225 230235 240 Glu Asn Asn Asn Thr Ser Lys Ile Asn Asp Thr Gly Ser Ala Thr Thr245 250 255 Ala Thr Thr Thr Thr Ala Thr Glu Thr Glu Ile Lys Pro Lys GluGlu 260 265 270 Asp Ala Thr Pro Ala Ser Leu His Gln Asp His Tyr Leu ValPro Tyr 275 280 285 Asn Gln Arg Ala Asn His Ser Lys Pro Ile Pro Pro PheLeu Leu Asp 290 295 300 Leu Asp Ser Gln Ser Val Pro Asp Ala Leu Lys LysGln Thr Asn Asp 305 310 315 320 Tyr Tyr Ile Leu Tyr Asn Pro Ala Leu ProArg Glu Ile Asp Val Glu 325 330 335 Leu His Lys Ser Leu Asp His Thr SerVal Val Cys Cys Val Lys Phe 340 345 350 Ser Asn Asp Gly Glu Tyr Leu AlaThr Gly Cys Asn Lys Thr Thr Gln 355 360 365 Val Tyr Arg Val Ser Asp GlySer Leu Val Ala Arg Leu Ser Asp Asp 370 375 380 Ser Ala Ala Asn Asn HisArg Asn Ser Ile Thr Glu Asn Asn Thr Thr 385 390 395 400 Thr Ser Thr AspAsn Asn Thr Met Thr Thr Thr Thr Thr Thr Thr Ile 405 410 415 Thr Thr ThrAla Met Thr Ser Ala Ala Glu Leu Ala Lys Asp Val Glu 420 425 430 Asn LeuAsn Thr Ser Ser Ser Pro Ser Ser Asp Leu Tyr Ile Arg Ser 435 440 445 ValCys Phe Ser Pro Asp Gly Lys Phe Leu Ala Thr Gly Ala Glu Asp 450 455 460Arg Leu Ile Arg Ile Trp Asp Ile Glu Asn Arg Lys Ile Val Met Ile 465 470475 480 Leu Gln Gly His Glu Gln Asp Ile Tyr Ser Leu Asp Tyr Phe Pro Ser485 490 495 Gly Asp Lys Leu Val Ser Gly Ser Gly Asp Arg Thr Val Arg IleTrp 500 505 510 Asp Leu Arg Thr Gly Gln Cys Ser Leu Thr Leu Ser Ile GluAsp Gly 515 520 525 Val Thr Thr Val Ala Val Ser Pro Gly Asp Gly Lys TyrIle Ala Ala 530 535 540 Gly Ser Leu Asp Arg Ala Val Arg Val Trp Asp SerGlu Thr Gly Phe 545 550 555 560 Leu Val Glu Arg Leu Asp Ser Glu Asn GluSer Gly Thr Gly His Lys 565 570 575 Asp Ser Val Tyr Ser Val Val Phe ThrArg Asp Gly Gln Ser Val Val 580 585 590 Ser Gly Ser Leu Asp Arg Ser ValLys Leu Trp Asn Leu Gln Asn Ala 595 600 605 Asn Asn Lys Ser Asp Ser LysThr Pro Asn Ser Gly Thr Cys Glu Val 610 615 620 Thr Tyr Ile Gly His LysAsp Phe Val Leu Ser Val Ala Thr Thr Gln 625 630 635 640 Asn Asp Glu TyrIle Leu Ser Gly Ser Lys Asp Arg Gly Val Leu Phe 645 650 655 Trp Asp LysLys Ser Gly Asn Pro Leu Leu Met Leu Gln Gly His Arg 660 665 670 Asn SerVal Ile Ser Val Ala Val Ala Asn Gly Ser Ser Leu Gly Pro 675 680 685 GluTyr Asn Val Phe Ala Thr Gly Ser Gly Asp Cys Lys Ala Arg Ile 690 695 700Trp Lys Tyr Lys Lys Ile Ala Pro Asn 705 710 (2) INFORMATION FOR SEQ IDNO:64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 798 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 HOMOLOG, Fig. 47 (xi) SEQUENCE DESCRIPTION: SEQID NO:64: Met Ser Gln Lys Gln Ser Thr Asn Gln Asn Gln Asn Gly Thr HisGln 1 5 10 15 Pro Gln Pro Val Lys Asn Gln Arg Thr Asn Asn Ala Ala GlyAla Asn 20 25 30 Ser Gly Gln Gln Pro Gln Gln Gln Ser Gln Gly Gln Ser GlnGln Gln 35 40 45 Gly Arg Ser Asn Gly Pro Phe Ser Ala Ser Asp Leu Asn ArgIle Val 50 55 60 Leu Glu Tyr Leu Asn Lys Lys Gly Tyr His Arg Thr Glu AlaMet Leu 65 70 75 80 Arg Ala Glu Ser Gly Arg Thr Leu Thr Pro Gln Asn LysGln Ser Pro 85 90 95 Ala Asn Thr Lys Thr Gly Lys Phe Pro Glu Gln Ser SerIle Pro Pro 100 105 110 Asn Pro Gly Lys Thr Ala Lys Pro Ile Ser Asn ProThr Asn Leu Ser 115 120 125 Ser Lys Arg Asp Ala Glu Gly Gly Ile Val SerSer Gly Arg Leu Glu 130 135 140 Gly Leu Asn Ala Pro Glu Asn Tyr Ile ArgAla Tyr Ser Met Leu Lys 145 150 155 160 Asn Trp Val Asp Ser Ser Leu GluIle Tyr Lys Pro Glu Leu Ser Tyr 165 170 175 Ile Met Tyr Pro Ile Phe IleTyr Leu Phe Leu Asn Leu Val Ala Lys 180 185 190 Asn Pro Val Tyr Ala ArgArg Phe Phe Asp Arg Phe Ser Pro Asp Phe 195 200 205 Lys Asp Phe His GlySer Glu Ile Asn Arg Leu Phe Ser Val Asn Ser 210 215 220 Ile Asp His IleLys Glu Asn Glu Val Ala Ser Ala Phe Gln Ser His 225 230 235 240 Lys TyrArg Ile Thr Met Ser Lys Thr Thr Leu Asn Leu Leu Leu Tyr 245 250 255 PheLeu Asn Glu Asn Glu Ser Ile Gly Gly Ser Leu Ile Ile Ser Val 260 265 270Ile Asn Gln His Leu Asp Pro Asn Ile Val Glu Ser Val Thr Ala Arg 275 280285 Glu Lys Leu Ala Asp Gly Ile Lys Val Leu Ser Asp Ser Glu Asn Gly 290295 300 Asn Gly Lys Gln Asn Leu Glu Met Asn Ser Val Pro Val Lys Leu Gly305 310 315 320 Pro Phe Pro Lys Asp Glu Glu Phe Val Lys Glu Ile Glu ThrGlu Leu 325 330 335 Lys Ile Lys Asp Asp Gln Glu Lys Gln Leu Asn Gln GlnThr Ala Gly 340 345 350 Asp Asn Tyr Ser Gly Ala Asn Asn Arg Thr Leu LeuGln Glu Tyr Lys 355 360 365 Ala Met Asn Asn Glu Lys Phe Lys Asp Asn ThrGly Asp Asp Asp Lys 370 375 380 Asp Lys Ile Lys Asp Lys Ile Ala Lys AspGlu Glu Lys Lys Glu Ser 385 390 395 400 Glu Leu Lys Val Asp Gly Glu LysLys Asp Ser Asn Leu Ser Ser Pro 405 410 415 Ala Arg Asp Ile Leu Pro LeuPro Pro Lys Thr Ala Leu Asp Leu Lys 420 425 430 Leu Glu Ile Gln Lys ValLys Glu Ser Arg Asp Ala Ile Lys Leu Asp 435 440 445 Asn Leu Gln Leu AlaLeu Pro Ser Val Cys Met Tyr Thr Phe Gln Asn 450 455 460 Thr Asn Lys AspMet Ser Cys Leu Asp Phe Ser Asp Asp Cys Arg Ile 465 470 475 480 Ala AlaAla Gly Phe Gln Asp Ser Tyr Ile Lys Ile Trp Ser Leu Asp 485 490 495 GlySer Ser Leu Asn Asn Pro Asn Ile Ala Leu Asn Asn Asn Asp Lys 500 505 510Asp Glu Asp Pro Thr Cys Lys Thr Leu Val Gly His Ser Gly Thr Val 515 520525 Tyr Ser Thr Ser Phe Ser Pro Asp Asn Lys Tyr Leu Leu Ser Gly Ser 530535 540 Glu Asp Lys Thr Val Arg Leu Trp Ser Met Asp Thr His Thr Ala Leu545 550 555 560 Val Ser Tyr Lys Gly His Asn His Pro Val Trp Asp Val SerPhe Ser 565 570 575 Pro Leu Gly His Tyr Phe Ala Thr Ala Ser His Asp GlnThr Ala Arg 580 585 590 Leu Trp Ser Cys Asp His Ile Tyr Pro Leu Arg IlePhe Ala Gly His 595 600 605 Leu Asn Asp Val Asp Cys Val Ser Phe His ProAsn Gly Cys Tyr Val 610 615 620 Phe Thr Gly Ser Ser Asp Lys Thr Cys ArgMet Trp Asp Val Ser Thr 625 630 635 640 Gly Asp Ser Val Arg Leu Phe LeuGly His Thr Ala Pro Val Ile Ser 645 650 655 Ile Ala Val Cys Pro Asp GlyArg Trp Leu Ser Thr Gly Ser Glu Asp 660 665 670 Gly Ile Ile Asn Val TrpAsp Ile Gly Thr Gly Lys Arg Leu Lys Gln 675 680 685 Met Arg Gly His GlyLys Asn Ala Ile Tyr Ser Leu Ser Tyr Ser Lys 690 695 700 Glu Gly Asn ValLeu Ile Ser Gly Gly Ala Asp His Thr Val Arg Val 705 710 715 720 Trp AspLeu Lys Lys Ala Thr Thr Glu Pro Ser Ala Glu Pro Asp Glu 725 730 735 ProPhe Ile Gly Tyr Leu Gly Asp Val Thr Ala Ser Ile Asn Gln Asp 740 745 750Ile Lys Glu Tyr Gly Arg Arg Arg Thr Val Ile Pro Thr Ser Asp Leu 755 760765 Val Ala Ser Phe Tyr Thr Lys Lys Thr Pro Val Phe Lys Val Lys Phe 770775 780 Ser Arg Ser Asn Leu Ala Leu Ala Gly Gly Ala Phe Arg Pro 785 790795 (2) INFORMATION FOR SEQ ID NO:65: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 439 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCU7, Fig. 48 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:65: Met Val Arg Arg Phe Arg Gly Lys Glu Leu AlaAla Thr Thr Phe Asn 1 5 10 15 Gly His Arg Asp Tyr Val Met Gly Ala PhePhe Ser His Asp Gln Glu 20 25 30 Lys Ile Tyr Thr Val Ser Lys Asp Gly AlaVal Phe Val Trp Glu Phe 35 40 45 Thr Lys Arg Pro Ser Asp Asp Asp Asp AsnGlu Ser Glu Asp Asp Asp 50 55 60 Lys Gln Glu Glu Val Asp Ile Ser Lys TyrSer Trp Arg Ile Thr Lys 65 70 75 80 Lys His Phe Phe Tyr Ala Asn Gln AlaLys Val Lys Cys Val Thr Phe 85 90 95 His Pro Ala Thr Arg Leu Leu Ala ValGly Phe Thr Ser Gly Glu Phe 100 105 110 Arg Leu Tyr Asp Leu Pro Asp PheThr Leu Ile Gln Gln Leu Ser Met 115 120 125 Gly Gln Asn Pro Val Asn ThrVal Ser Val Asn Gln Thr Gly Glu Trp 130 135 140 Leu Ala Phe Gly Ser SerLys Leu Gly Gln Leu Leu Val Tyr Glu Trp 145 150 155 160 Gln Ser Glu SerTyr Ile Leu Lys Gln Gln Gly His Phe Asp Ser Thr 165 170 175 Asn Ser LeuAla Tyr Ser Pro Asp Gly Ser Arg Val Val Thr Ala Ser 180 185 190 Glu AspGly Lys Ile Lys Val Trp Asp Ile Thr Ser Gly Phe Cys Leu 195 200 205 AlaThr Phe Glu Glu His Thr Ser Ser Val Thr Ala Val Gln Phe Ala 210 215 220Lys Arg Gly Gln Val Met Phe Ser Ser Ser Leu Asp Gly Thr Val Arg 225 230235 240 Ala Trp Asp Leu Ile Arg Tyr Arg Asn Phe Arg Thr Phe Thr Gly Thr245 250 255 Glu Arg Ile Gln Phe Asn Cys Leu Ala Val Asp Pro Ser Gly GluVal 260 265 270 Val Cys Ala Gly Ser Leu Asp Asn Phe Asp Ile His Val TrpSer Val 275 280 285 Gln Thr Gly Gln Leu Leu Asp Ala Leu Ser Gly His GluGly Pro Val 290 295 300 Ser Cys Leu Ser Phe Ser Gln Glu Asn Ser Val LeuAla Ser Ala Ser 305 310 315 320 Trp Asp Lys Thr Ile Arg Ile Trp Ser IlePhe Gly Arg Ser Gln Gln 325 330 335 Val Glu Pro Ile Glu Val Tyr Ser AspVal Leu Ala Leu Ser Met Arg 340 345 350 Pro Asp Gly Lys Glu Val Ala ValSer Thr Leu Lys Gly Gln Ile Ser 355 360 365 Ile Phe Asn Ile Glu Asp AlaLys Gln Val Gly Asn Ile Asp Cys Arg 370 375 380 Lys Asp Ile Ile Ser GlyArg Phe Asn Gln Asp Arg Phe Thr Ala Lys 385 390 395 400 Ile Leu Asn AspPro Asn Phe Leu Leu Gln Tyr Ile Thr Val Leu Met 405 410 415 Val Trp LeuLeu Trp Leu Val Val Ile Ile Thr Pro Phe Val Tyr Met 420 425 430 Met PheGln Met Lys Ser Cys 435 (2) INFORMATION FOR SEQ ID NO:66: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 514 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCW2PROTEIN, Fig. 49 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:66: Met Ser ThrLeu Ile Pro Pro Pro Ser Lys Lys Gln Lys Lys Glu Ala 1 5 10 15 Gln LeuPro Arg Glu Val Ala Ile Ile Pro Lys Asp Leu Pro Asn Val 20 25 30 Ser IleLys Phe Gln Ala Leu Asp Thr Gly Asp Asn Val Gly Gly Ala 35 40 45 Leu ArgVal Pro Gly Ala Ile Ser Glu Lys Gln Leu Glu Glu Leu Leu 50 55 60 Asn GlnLeu Asn Gly Thr Ser Asp Asp Pro Val Pro Tyr Thr Phe Ser 65 70 75 80 CysThr Ile Gln Gly Lys Lys Ala Ser Asp Pro Val Lys Thr Ile Asp 85 90 95 IleThr Asp Asn Leu Tyr Ser Ser Leu Ile Lys Pro Gly Tyr Asn Ser 100 105 110Thr Glu Asp Gln Ile Thr Leu Leu Tyr Thr Pro Arg Ala Val Phe Lys 115 120125 Val Lys Pro Val Thr Arg Ser Ser Ser Ala Ile Ala Gly His Gly Ser 130135 140 Thr Ile Leu Cys Ser Ala Phe Ala Pro His Thr Ser Ser Arg Met Val145 150 155 160 Thr Gly Ala Gly Asp Asn Thr Ala Arg Ile Trp Asp Cys AspThr Gln 165 170 175 Thr Pro Met His Thr Leu Lys Gly His Tyr Asn Trp ValLeu Cys Val 180 185 190 Ser Trp Ser Pro Asp Gly Glu Val Ile Ala Thr GlySer Met Asp Asn 195 200 205 Thr Ile Arg Leu Trp Asp Pro Lys Ser Gly GlnCys Leu Gly Asp Ala 210 215 220 Leu Arg Gly His Ser Lys Trp Ile Thr SerLeu Ser Trp Glu Pro Ile 225 230 235 240 His Leu Val Lys Pro Gly Ser LysPro Arg Leu Ala Ser Ser Ser Lys 245 250 255 Asp Gly Thr Ile Lys Ile TrpAsp Thr Val Ser Arg Val Cys Gln Tyr 260 265 270 Thr Met Ser Gly His ThrAsn Ser Val Ser Cys Val Lys Trp Gly Gly 275 280 285 Gln Gly Leu Leu TyrSer Gly Ser His Asp Arg Thr Val Arg Val Trp 290 295 300 Asp Ile Asn SerGln Gly Arg Cys Ile Asn Ile Leu Lys Ser His Ala 305 310 315 320 His TrpVal Asn His Leu Ser Leu Ser Thr Asp Tyr Ala Leu Arg Ile 325 330 335 GlyAla Phe Asp His Thr Gly Lys Lys Pro Ser Thr Pro Glu Glu Ala 340 345 350Gln Lys Lys Ala Leu Glu Asn Tyr Glu Lys Ile Cys Lys Lys Asn Gly 355 360365 Asn Ser Glu Glu Met Met Val Thr Ala Ser Asp Asp Tyr Thr Met Phe 370375 380 Leu Trp Asn Pro Leu Lys Ser Thr Lys Pro Ile Ala Arg Met Thr Gly385 390 395 400 His Gln Lys Leu Val Asn His Val Ala Phe Ser Pro Asp GlyArg Tyr 405 410 415 Ile Val Ser Ala Ser Phe Asp Asn Ser Ile Lys Leu TrpAsp Gly Arg 420 425 430 Asp Gly Lys Phe Ile Ser Thr Phe Arg Gly His IleAla Ser Val Tyr 435 440 445 Gln Val Ala Trp Ser Ser Asp Cys Arg Leu LeuVal Ser Cys Ser Lys 450 455 460 Asp Thr Thr Leu Lys Val Trp Asp Val ArgThr Arg Lys Leu Ser Val 465 470 475 480 Asp Leu Pro Gly Ile Lys Thr LysLeu Tyr Val Asp Trp Ser Val Asp 485 490 495 Gly Lys Arg Val Cys Ser GlyGly Lys Asp Lys Met Val Arg Leu Trp 500 505 510 Thr His (2) INFORMATIONFOR SEQ ID NO:67: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 852 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:protein (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: YKL525, Fig. 50 (xi) SEQUENCE DESCRIPTION: SEQID NO:67: Met Phe Lys Ser Lys Thr Ser Thr Leu Ser Tyr Asp Glu Thr ProAsn 1 5 10 15 Ser Asn Glu Gly Asp Arg Asn Ala Thr Pro Val Asn Pro LysGlu Lys 20 25 30 Ser Gln Thr Lys His Leu Asn Ile Pro Gly Asp Arg Ser ArgHis Ser 35 40 45 Ser Ile Ala Asp Ser Lys Arg Ser Ser Ser Arg Tyr Asp GlyGly Tyr 50 55 60 Ser Ala Asp Ile Ile Pro Ala Gln Leu Arg Phe Ile Asp AsnIle Asp 65 70 75 80 Tyr Gly Thr Arg Leu Arg Lys Thr Leu His Arg Asn SerVal Val Ser 85 90 95 Asn Gly Tyr Asn Lys Leu Ser Glu Asn Asp Arg Trp TyrPhe Asp Leu 100 105 110 Phe Asp Arg Lys Tyr Phe Glu Asn Tyr Leu Glu GluPro Thr Tyr Ile 115 120 125 Lys Ile Phe Lys Lys Lys Glu Gly Leu Glu GlnPhe Asp Arg Met Phe 130 135 140 Leu Ala Gln Glu Leu Lys Ile Pro Asp ValTyr Lys Ser Thr Thr Tyr 145 150 155 160 Gln Gly Glu Pro Ala Val Ala AsnSer Glu Leu Phe Lys Asn Ser Ile 165 170 175 Cys Cys Cys Thr Phe Ser HisAsp Gly Lys Tyr Met Val Ile Gly Cys 180 185 190 Lys Asp Gly Ser Leu HisLeu Trp Lys Val Ile Asn Ser Pro Val Lys 195 200 205 Arg Ser Glu Met GlyArg Ser Glu Lys Ser Val Ser Ala Ser Arg Ala 210 215 220 Asn Ser Leu LysIle Gln Arg His Leu Ala Ser Ile Ser Ser His Asn 225 230 235 240 Gly SerIle Ser Ser Asn Asp Leu Lys Pro Ser Asp Gln Phe Glu Gly 245 250 255 ProSer Lys Gln Leu His Leu Tyr Ala Pro Val Phe Tyr Ser Asp Val 260 265 270Phe Arg Val Phe Met Glu His Ala Leu Asp Ile Leu Asp Ala Asn Trp 275 280285 Ser Lys Asn Gly Phe Leu Ile Thr Ala Ser Met Asp Lys Thr Ala Lys 290295 300 Leu Trp His Pro Glu Arg Lys Tyr Ser Leu Lys Thr Phe Val His Pro305 310 315 320 Asp Phe Val Thr Ser Ala Ile Phe Phe Pro Asn Asp Asp ArgPhe Ile 325 330 335 Ile Thr Gly Cys Leu Asp His Arg Cys Arg Leu Trp SerIle Leu Asp 340 345 350 Asn Glu Val Ser Tyr Ala Phe Asp Cys Lys Asp LeuIle Thr Ser Leu 355 360 365 Thr Leu Ser Pro Pro Gly Gly Glu Tyr Thr IleIle Gly Thr Phe Asn 370 375 380 Gly Tyr Ile Tyr Val Leu Leu Thr His GlyLeu Lys Phe Val Ser Ser 385 390 395 400 Phe His Val Ser Asp Lys Ser ThrGln Gly Thr Thr Lys Asn Ser Phe 405 410 415 His Pro Ser Ser Glu Tyr GlyLys Val Gln His Gly Pro Arg Ile Thr 420 425 430 Gly Leu Gln Cys Phe PheSer Lys Val Asp Lys Asn Leu Arg Leu Ile 435 440 445 Val Thr Thr Asn AspSer Lys Ile Gln Ile Phe Asp Leu Asn Glu Lys 450 455 460 Lys Pro Leu GluLeu Phe Lys Gly Phe Gln Ser Gly Ser Ser Arg His 465 470 475 480 Arg GlyGln Phe Leu Met Met Lys Asn Glu Pro Val Val Phe Thr Gly 485 490 495 SerAsp Asp His Trp Phe Tyr Thr Trp Lys Met Gln Ser Phe Asn Leu 500 505 510Ser Ala Glu Met Asn Cys Thr Ala Pro His Arg Lys Lys Arg Leu Ser 515 520525 Gly Ser Met Ser Leu Lys Gly Leu Leu Arg Ile Val Ser Asn Lys Ser 530535 540 Thr Asn Asp Glu Cys Leu Thr Glu Thr Ser Asn Gln Ser Ser Ser His545 550 555 560 Thr Phe Thr Asn Ser Ser Lys Asn Val Leu Gln Thr Gln ThrVal Gly 565 570 575 Ser Gln Ala Ile Lys Asn Asn His Tyr Ile Ser Phe HisAla His Asn 580 585 590 Ser Pro Val Thr Cys Ala Ser Ile Ala Pro Asp ValAla Ile Lys Asn 595 600 605 Leu Ser Leu Ser Asn Asp Leu Ile Phe Glu LeuThr Ser Gln Tyr Phe 610 615 620 Lys Glu Met Gly Gln Asn Tyr Ser Glu SerLys Glu Thr Cys Asp Asn 625 630 635 640 Lys Pro Asn His Pro Val Thr GluThr Gly Gly Phe Ser Ser Asn Leu 645 650 655 Ser Asn Val Val Asn Asn ValGly Thr Ile Leu Ile Thr Thr Asp Ser 660 665 670 Gln Gly Leu Ile Arg ValPhe Arg Thr Asp Ile Leu Pro Glu Ile Arg 675 680 685 Lys Lys Ile Ile GluLys Phe His Glu Tyr Asn Leu Phe His Leu Glu 690 695 700 Ala Ala Gly LysIle Asn Asn His Asn Asn Asp Ser Ile Leu Glu Asn 705 710 715 720 Arg MetAsp Glu Arg Ser Ser Thr Glu Asp Asn Glu Phe Ser Thr Thr 725 730 735 ProPro Ser Asn Thr His Asn Ser Arg Pro Ser His Asp Phe Cys Glu 740 745 750Leu His Pro Asn Asn Ser Pro Val Ile Ser Gly Met Pro Ser Arg Ala 755 760765 Ser Ala Ile Phe Lys Asn Ser Ile Phe Asn Lys Ser Asn Gly Ser Phe 770775 780 Ile Ser Leu Lys Ser Arg Ser Glu Ser Thr Ser Ser Thr Val Phe Gly785 790 795 800 Pro His Asp Ile Pro Arg Val Ser Thr Thr Tyr Pro Lys LeuLys Cys 805 810 815 Asp Val Cys Asn Gly Ser Asn Phe Glu Cys Ala Ser LysAsn Pro Ile 820 825 830 Ala Gly Gly Asp Ser Gly Phe Thr Cys Ala Asp CysGly Thr Ile Leu 835 840 845 Asn Asn Phe Arg 850 (2) INFORMATION FOR SEQID NO:68: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 798 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: yrb 1410 yeast, Fig. 51 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:68: Met Ser Gln Lys Gln Ser Thr Asn Gln Asn Gln Asn Gly ThrHis Gln 1 5 10 15 Pro Gln Pro Val Lys Asn Gln Arg Thr Asn Asn Ala AlaGly Ala Asn 20 25 30 Ser Gly Gln Gln Pro Gln Gln Gln Ser Gln Gly Gln SerGln Gln Gln 35 40 45 Gly Arg Ser Asn Gly Pro Phe Ser Ala Ser Asp Leu AsnArg Ile Val 50 55 60 Leu Glu Tyr Leu Asn Lys Lys Gly Tyr His Arg Thr GluAla Met Leu 65 70 75 80 Arg Ala Glu Ser Gly Arg Thr Leu Thr Pro Gln AsnLys Gln Ser Pro 85 90 95 Ala Asn Thr Lys Thr Gly Lys Phe Pro Glu Gln SerSer Ile Pro Pro 100 105 110 Asn Pro Gly Lys Thr Ala Lys Pro Ile Ser AsnPro Thr Asn Leu Ser 115 120 125 Ser Lys Arg Asp Ala Glu Gly Gly Ile ValSer Ser Gly Arg Leu Glu 130 135 140 Gly Leu Asn Ala Pro Glu Asn Tyr IleArg Ala Tyr Ser Met Leu Lys 145 150 155 160 Asn Trp Val Asp Ser Ser LeuGlu Ile Tyr Lys Pro Glu Leu Ser Tyr 165 170 175 Ile Met Tyr Pro Ile PheIle Tyr Leu Phe Leu Asn Leu Val Ala Lys 180 185 190 Asn Pro Val Tyr AlaArg Arg Phe Phe Asp Arg Phe Ser Pro Asp Phe 195 200 205 Lys Asp Phe HisGly Ser Glu Ile Asn Arg Leu Phe Ser Val Asn Ser 210 215 220 Ile Asp HisIle Lys Glu Asn Glu Val Ala Ser Ala Phe Gln Ser His 225 230 235 240 LysTyr Arg Ile Thr Met Ser Lys Thr Thr Leu Asn Leu Leu Leu Tyr 245 250 255Phe Leu Asn Glu Asn Glu Ser Ile Gly Gly Ser Leu Ile Ile Ser Val 260 265270 Ile Asn Gln His Leu Asp Pro Asn Ile Val Glu Ser Val Thr Ala Arg 275280 285 Glu Lys Leu Ala Asp Gly Ile Lys Val Leu Ser Asp Ser Glu Asn Gly290 295 300 Asn Gly Lys Gln Asn Leu Glu Met Asn Ser Val Pro Val Lys LeuGly 305 310 315 320 Pro Phe Pro Lys Asp Glu Glu Phe Val Lys Glu Ile GluThr Glu Leu 325 330 335 Lys Ile Lys Asp Asp Gln Glu Lys Gln Leu Asn GlnGln Thr Ala Gly 340 345 350 Asp Asn Tyr Ser Gly Ala Asn Asn Arg Thr LeuLeu Gln Glu Tyr Lys 355 360 365 Ala Met Asn Asn Glu Lys Phe Lys Asp AsnThr Gly Asp Asp Asp Lys 370 375 380 Asp Lys Ile Lys Asp Lys Ile Ala LysAsp Glu Glu Lys Lys Glu Ser 385 390 395 400 Glu Leu Lys Val Asp Gly GluLys Lys Asp Ser Asn Leu Ser Ser Pro 405 410 415 Ala Arg Asp Ile Leu ProLeu Pro Pro Lys Thr Ala Leu Asp Leu Lys 420 425 430 Leu Glu Ile Gln LysVal Lys Glu Ser Arg Asp Ala Ile Lys Leu Asp 435 440 445 Asn Leu Gln LeuAla Leu Pro Ser Val Cys Met Tyr Thr Phe Gln Asn 450 455 460 Thr Asn LysAsp Met Ser Cys Leu Asp Phe Ser Asp Asp Cys Arg Ile 465 470 475 480 AlaAla Ala Gly Phe Gln Asp Ser Tyr Ile Lys Ile Trp Ser Leu Asp 485 490 495Gly Ser Ser Leu Asn Asn Pro Asn Ile Ala Leu Asn Asn Asn Asp Lys 500 505510 Asp Glu Asp Pro Thr Cys Lys Thr Leu Val Gly His Ser Gly Thr Val 515520 525 Tyr Ser Thr Ser Phe Ser Pro Asp Asn Lys Tyr Leu Leu Ser Gly Ser530 535 540 Glu Asp Lys Thr Val Arg Leu Trp Ser Met Asp Thr His Thr AlaLeu 545 550 555 560 Val Ser Tyr Lys Gly His Asn His Pro Val Trp Asp ValSer Phe Ser 565 570 575 Pro Leu Gly His Tyr Phe Ala Thr Ala Ser His AspGln Thr Ala Arg 580 585 590 Leu Trp Ser Cys Asp His Ile Tyr Pro Leu ArgIle Phe Ala Gly His 595 600 605 Leu Asn Asp Val Asp Cys Val Ser Phe HisPro Asn Gly Cys Tyr Val 610 615 620 Phe Thr Gly Ser Ser Asp Lys Thr CysArg Met Trp Asp Val Ser Thr 625 630 635 640 Gly Asp Ser Val Arg Leu PheLeu Gly His Thr Ala Pro Val Ile Ser 645 650 655 Ile Ala Val Cys Pro AspGly Arg Trp Leu Ser Thr Gly Ser Glu Asp 660 665 670 Gly Ile Ile Asn ValTrp Asp Ile Gly Thr Gly Lys Arg Leu Lys Gln 675 680 685 Met Arg Gly HisGly Lys Asn Ala Ile Tyr Ser Leu Ser Tyr Ser Lys 690 695 700 Glu Gly AsnVal Leu Ile Ser Gly Gly Ala Asp His Thr Val Arg Val 705 710 715 720 TrpAsp Leu Lys Lys Ala Thr Thr Glu Pro Ser Ala Glu Pro Asp Glu 725 730 735Pro Phe Ile Gly Tyr Leu Gly Asp Val Thr Ala Ser Ile Asn Gln Asp 740 745750 Ile Lys Glu Tyr Gly Arg Arg Arg Thr Val Ile Pro Thr Ser Asp Leu 755760 765 Val Ala Ser Phe Tyr Thr Lys Lys Thr Pro Val Phe Lys Val Lys Phe770 775 780 Ser Arg Ser Asn Leu Ala Leu Ala Gly Gly Ala Phe Arg Pro 785790 795 (2) INFORMATION FOR SEQ ID NO:69: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RACK1 protein rI, Fig. 1C(xi) SEQUENCE DESCRIPTION: SEQ ID NO:69: Gly His Asn Gly Trp Val Thr GlnIle Ala Thr Thr Pro Gln Phe Pro 1 5 10 15 Asp Met Ile Leu Ser Ala SerArg Asp Lys Thr Ile Ile Met Trp Lys 20 25 30 (2) INFORMATION FOR SEQ IDNO:70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 protein rII, Fig. 1C (xi) SEQUENCEDESCRIPTION: SEQ ID NO:70: Gly His Ser His Phe Val Ser Asp Val Val IleSer Ser Asp Gly Gln 1 5 10 15 Phe Ala Leu Ser Gly Ser Trp Asp Gly ThrLeu Arg Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:71: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 protein rIII, Fig. 1C (xi) SEQUENCEDESCRIPTION: SEQ ID NO:71: Gly His Thr Lys Asp Val Leu Ser Val Ala PheSer Ser Asp Asn Arg 1 5 10 15 Gln Ile Val Ser Gly Ser Arg Asp Lys ThrIle Lys Leu Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:72: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 protein rIV, Fig. 1C (xi) SEQUENCEDESCRIPTION: SEQ ID NO:72: Ser His Ser Glu Trp Val Ser Cys Val Arg PheSer Pro Asn Ser Ser 1 5 10 15 Asn Pro Ile Ile Val Ser Cys Gly Trp AspLys Leu Val Lys Val Trp 20 25 30 Asn (2) INFORMATION FOR SEQ ID NO:73:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RACK1 protein rV, Fig. 1C (xi) SEQUENCE DESCRIPTION:SEQ ID NO:73: Gly His Thr Gly Tyr Leu Asn Thr Val Thr Val Ser Pro AspGly Ser 1 5 10 15 Leu Cys Ala Ser Gly Gly Lys Asp Gly Gln Ala Met LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:74: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RACK1protein rVI, Fig. 1C (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74: Leu AspGly Gly Asp Ile Ile Asn Ala Leu Cys Phe Ser Pro Asn Arg 1 5 10 15 TyrTrp Leu Cys Ala Ala Thr Gly Pro Ser Ile Lys Ile Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:75: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: RACK1 protein rVII, Fig. 1C (xi)SEQUENCE DESCRIPTION: SEQ ID NO:75: Ser Lys Ala Glu Pro Pro Gln Cys ThrSer Leu Ala Trp Ser Ala Asp 1 5 10 15 Gly Gln Thr Leu Phe Ala Gly TyrThr Asp Asn Leu Val Arg Val Trp 20 25 30 Gln (2) INFORMATION FOR SEQ IDNO:76: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Human 55 kDa protein rI, Fig. 11 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:76: Gly His Thr Asp Ala Val Leu Asp Leu Ser TrpAsn Lys Leu Ile Arg 1 5 10 15 Asn Val Leu Ala Ser Ala Ser Ala Asp AsnThr Val Ile Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:77: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Human 55 kDa protein rII, Fig. 11 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:77: Ala His Asn Asp Glu Ile Ser Gly Leu Asp LeuSer Ser Gln Ile Lys 1 5 10 15 Gly Cys Leu Val Thr Ala Ser Ala Asp LysTyr Val Lys Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:78: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Human 55 kDa protein rIII, Fig. 11 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:78: Val His Ser Arg Asp Met Lys Met Gly Val LeuPhe Cys Ser Ser Cys 1 5 10 15 Cys Pro Asp Leu Pro Phe Ile Tyr Ala PheGly Gly Gln Lys Glu Gly 20 25 30 Leu Arg Val Trp Asp 35 (2) INFORMATIONFOR SEQ ID NO:79: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: AAC-RICH protein rI, Fig. 12 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:79: Gly Asn Lys Lys Lys Ser Thr Ser Val Ala TrpAsn Ala Asn Gly Thr 1 5 10 15 Lys Ile Ala Ser Ser Gly Ser Asp Gly IleVal Arg Val Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:80: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: AAC-RICH protein rII, Fig. 12 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:80: Gly His Asp Gly Ser Ile Glu Lys Ile Ser TrpSer Pro Lys Asn Asn 1 5 10 15 Asp Leu Leu Ala Ser Ala Gly Thr Asp LysVal Ile Lys Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:81: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: AAC-RICH protein rIII, Fig. 12 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:81: Asp His Leu Ala Leu Ile Asp Leu Pro Thr IleLys Thr Leu Lys Ile 1 5 10 15 Tyr Lys Phe Asn Gly Glu Glu Leu Asn GlnVal Gly Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:82: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:AAC-RICH protein rIV, Fig. 12 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82:Gly His Thr Ala Ser Ile Tyr Cys Met Glu Phe Asp Pro Thr Gly Lys 1 5 1015 Tyr Leu Ala Ala Gly Ser Ala Asp Ser Ile Val Ser Leu Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:83: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 34 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: BETA TRCP rI, Fig. 13 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:83: Ile His Cys Arg Ser Glu Thr Ser LysGly Val Tyr Cys Leu Gln Tyr 1 5 10 15 Asp Asp Gln Lys Ile Val Ser GlyLeu Arg Asp Asn Thr Ile Lys Ile 20 25 30 Trp Asp (2) INFORMATION FOR SEQID NO:84: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: BETA TRCP rII, Fig. 13 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:84: Gly His Thr Gly Ser Val Leu Cys Leu Gln Tyr Asp Glu ArgVal Ile 1 5 10 15 Ile Thr Gly Ser Asp Ser Thr Val Arg Val Trp Asp 20 25(2) INFORMATION FOR SEQ ID NO:85: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: BETA TRCP rIII, Fig. 13 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:85: Ile His His Cys Glu Ala Val Leu HisLeu Arg Phe Asn Asn Gly Met 1 5 10 15 Met Val Thr Cys Ser Lys Asp ArgSer Ile Ala Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:86: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: BETA TRCP rIV, Fig. 13 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:86: Gly His Arg Ala Ala Val Asn Val Val Asp Phe Asp Asp LysTyr Ile 1 5 10 15 Val Ser Ala Ser Gly Asp Arg Thr Ile Lys Val Trp Asn 2025 (2) INFORMATION FOR SEQ ID NO:87: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: BETA TRCP rV, Fig. 13 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:87: Gly His Lys Arg Gly Ile Ala Cys LeuGln Tyr Arg Asp Arg Leu Val 1 5 10 15 Val Ser Gly Ser Ser Asp Asn ThrIle Arg Leu Trp Asp 20 25 (2) INFORMATION FOR SEQ ID NO:88: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: BETATRCP rVI, Fig. 13 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:88: Gly His GluGlu Leu Val Arg Cys Ile Arg Phe Asp Asn Lys Arg Ile 1 5 10 15 Val SerGly Ala Tyr Asp Gly Lys Ile Lys Val Trp Asp 20 25 (2) INFORMATION FORSEQ ID NO:89: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: BETA TRCP rVII, Fig. 13 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:89: Glu His Ser Gly Arg Val Phe Arg Leu Gln Phe Asp Glu PheGln Ile 1 5 10 15 Val Ser Ser Ser His Asp Asp Thr Ile Leu Ile Trp Asp 2025 (2) INFORMATION FOR SEQ ID NO:90: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: beta-prime-cop rI, Fig. 14 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:90: Ala His Ser Asp Tyr Ile Arg Cys IleAla Val His Pro Thr Gln Pro 1 5 10 15 Phe Ile Leu Thr Ser Ser Asp AspMet Leu Ile Lys Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:91:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: beta-prime-cop rII, Fig. 14 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:91: Gly His Thr His Tyr Val Met Gln Ile Val IleAsn Pro Lys Asp Asn 1 5 10 15 Asn Gln Phe Ala Ser Ala Ser Leu Asp ArgThr Ile Lys Val Trp Gln 20 25 30 (2) INFORMATION FOR SEQ ID NO:92: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: beta-prime-cop rIII, Fig. 14 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:92: Gly His Glu Lys Gly Val Asn Cys Ile Asp TyrTyr Ser Gly Gly Asp 1 5 10 15 Lys Pro Tyr Leu Ile Ser Gly Ala Asp AspArg Leu Val Lys Ile Trp 20 25 30 Asp (2) INFORMATION FOR SEQ ID NO:93:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: beta-prime-cop rIV, Fig. 14 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:93: Gly His Ala Gln Asn Val Ser Cys Ala Ser PheHis Pro Glu Leu Pro 1 5 10 15 Ile Ile Ile Thr Gly Ser Glu Asp Gly ThrVal Arg Ile Trp His 20 25 30 (2) INFORMATION FOR SEQ ID NO:94: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CDC4 / CDC20 protein rI, Fig. 15 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:94: Gly His Met Thr Ser Val Ile Thr Cys Leu GlnPhe Glu Asp Asn Tyr 1 5 10 15 Val Ile Thr Gly Ala Asp Asp Lys Met IleArg Val Tyr Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:95: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: CDC4 /CDC20 protein rII, Fig. 15 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:95: GlyHis Asp Gly Gly Val Trp Ala Leu Lys Tyr Ala His Gly Gly Ile 1 5 10 15Leu Val Ser Gly Ser Thr Asp Arg Thr Val Arg Val Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:96: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: CDC4 / CDC20 protein rIII, Fig. 15 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:96: Gly His Asn Ser Thr Val Arg Cys LeuAsp Ile Val Glu Tyr Lys Asn 1 5 10 15 Ile Lys Tyr Ile Val Thr Gly SerArg Asp Asn Thr Leu His Val Trp 20 25 30 Lys (2) INFORMATION FOR SEQ IDNO:97: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CDC4 / CDC20 protein rIV, Fig. 15 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:97: Gly His Met Ala Ser Val Arg Thr Val Ser GlyHis Gly Asn Ile Val 1 5 10 15 Val Ser Gly Ser Tyr Asp Asn Thr Leu IleVal Trp Asp 20 25 (2) INFORMATION FOR SEQ ID NO:98: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: CDC4 /CDC20 protein rV, Fig. 15 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:98: GlyHis Thr Asp Arg Ile Tyr Ser Thr Ile Tyr Asp His Glu Arg Lys 1 5 10 15Arg Cys Ile Ser Ala Ser Met Asp Thr Thr Ile Arg Ile Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:99: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: CDC4 / CDC20 protein rVI, Fig. 15 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:99: Gly His Thr Ala Leu Val Gly Leu LeuArg Leu Ser Asp Lys Phe Leu 1 5 10 15 Val Ser Ala Ala Ala Asp Gly SerIle Arg Gly Trp Asp 20 25 (2) INFORMATION FOR SEQ ID NO:100: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP-CHLAMIDOMONAS HOMOLOG rI, Fig. 16 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:100: Gly His Thr Asn Trp Val Thr Ala Ile Ala ThrPro Leu Asp Pro Ser 1 5 10 15 Ser Asn Thr Leu Leu Ser Ala Ser Arg AspLys Ser Val Leu Val Trp 20 25 30 Glu (2) INFORMATION FOR SEQ ID NO:101:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rII, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:101: Gly His Ser His Phe Val Gln Asp ValVal Ile Ser Ser Asp Gly Gln 1 5 10 15 Phe Cys Leu Thr Gly Ser Trp AspGly Thr Leu Arg Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:102:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rIII, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:102: Gly His Thr Lys Asp Val Leu Ser ValAla Phe Ser Val Asp Asn Arg 1 5 10 15 Gln Ile Val Ser Gly Ser Arg AspLys Thr Ile Lys Leu Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:103:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rIV, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:103: Gly His Thr Glu Trp Val Ser Cys ValArg Phe Ser Pro Met Thr Thr 1 5 10 15 Asn Pro Ile Ile Val Ser Gly GlyTrp Asp Lys Met Val Lys Val Trp 20 25 30 Asn (2) INFORMATION FOR SEQ IDNO:104: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rV, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:104: Gly His His Gly Tyr Val Asn Thr ValThr Val Ser Pro Asp Gly Ser 1 5 10 15 Leu Cys Ala Ser Gly Gly Lys AspGly Ile Ala Met Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:105:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rVI, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:105: Ile His Cys Leu Cys Phe Ser Pro AsnArg Tyr Trp Leu Cys Ala Ala 1 5 10 15 Thr Gln Ser Ser Ile Lys Ile TrpAsp Leu Glu Ser Lys Ser Ile Val 20 25 30 (2) INFORMATION FOR SEQ IDNO:106: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GBLP -CHLAMIDOMONAS HOMOLOG rVII, Fig. 16 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:106: Lys Lys Ala Gln Val Pro Tyr Cys ValSer Leu Ala Trp Ser Ala Asp 1 5 10 15 Gly Ser Thr Leu Tyr Ser Gly TyrThr Asp Gly Gln Ile Arg Val Trp 20 25 30 Ala (2) INFORMATION FOR SEQ IDNO:107: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: cop-1 protein rI, Fig. 17 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:107: Met Ser Thr Arg Ser Lys Leu Ser Cys Leu Ser Trp Asn LysHis Glu 1 5 10 15 Lys Asn His Ile Ala Ser Ser Asp Tyr Glu Gly Ile ValThr Val Trp 20 25 30 Asp (2) INFORMATION FOR SEQ ID NO:108: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: cop-1protein rII, Fig. 17 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:108: Glu LysArg Ala Trp Ser Val Asp Phe Ser Arg Thr Glu Pro Ser Met 1 5 10 15 LeuVal Ser Gly Ser Asp Asp Cys Lys Val Lys Val Trp Cys 20 25 30 (2)INFORMATION FOR SEQ ID NO:109: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: cop-1 protein rIII, Fig. 17 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:109: Gly His Lys Lys Ala Val Ser Tyr MetLys Phe Leu Ser Asn Asn Glu 1 5 10 15 Leu Ala Ser Ala Ser Thr Asp SerThr Leu Arg Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:110: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Coronin (p55) rI, Fig. 19 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:110: Gly His Lys Ser Ala Val Leu Asp Ile Ala Phe His Pro PheAsn Glu 1 5 10 15 Asn Leu Val Gly Ser Val Ser Glu Asp Cys Asn Ile CysIle Trp Gly 20 25 30 (2) INFORMATION FOR SEQ ID NO:111: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:Coronin (p55) rII, Fig. 19 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:111: GlyHis Lys Arg Lys Val Gly Thr Ile Ser Phe Gly Pro Val Ala Asp 1 5 10 15Asn Val Ala Val Thr Ser Ser Gly Asp Phe Leu Val Lys Thr Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:112: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: Coronin (p55) rIII, Fig. 19(xi) SEQUENCE DESCRIPTION: SEQ ID NO:112: Gly His Ser Asp Met Ile ThrSer Cys Glu Trp Asn His Asn Gly Ser 1 5 10 15 Gln Ile Val Thr Thr CysLys Asp Lys Lys Ala Arg Val Phe Asp 20 25 30 (2) INFORMATION FOR SEQ IDNO:113: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CORO PROTEIN rI, Fig. 18 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:113: Arg His Val Phe Ala Ala Gln Pro Lys Lys Glu Glu Cys TyrGln Asn 1 5 10 15 Leu Lys Thr Lys Ser Ala Val Trp Asp Ser Asn Tyr ValAla Ala Asn 20 25 30 Thr Arg Tyr Ile Trp Asp 35 (2) INFORMATION FOR SEQID NO:114: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CORO PROTEIN rII, Fig. 18 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:114: Gly His Lys Ser Ala Val Leu Asp Ile Ala Phe His Pro PheAsn Glu 1 5 10 15 Asn Leu Val Gly Ser Val Ser Glu Asp Cys Asn Ile CysIle Trp Gly 20 25 30 (2) INFORMATION FOR SEQ ID NO:115: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: COROPROTEIN rIII, Fig. 18 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:115: Gly HisLys Arg Lys Val Gly Thr Ile Ser Phe Gly Pro Val Ala Asp 1 5 10 15 AsnVal Ala Val Thr Ser Ser Gly Asp Phe Leu Val Lys Thr Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:116: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:29 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: CORO PROTEIN rIV, Fig. 18 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:116: Gly His Ser Asp Met Ile Thr Ser Cys Glu HisAsn Gly Ser Gln Ile 1 5 10 15 Val Thr Thr Cys Lys Asp Lys Lys Ala ArgVal Phe Asp 20 25 (2) INFORMATION FOR SEQ ID NO:117: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: CSTF50kDa rI, Fig. 20 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:117: Asp His ValAsp Glu Val Thr Cys Leu Ala Phe His Pro Thr Glu Gln 1 5 10 15 Ile LeuAla Ser Gly Ser Arg Asp Tyr Thr Leu Lys Leu Phe Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:118: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: CSTF 50kDa rII, Fig. 20 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:118: Asp His Val Asp Glu Val Thr Cys Leu Ala PheHis Pro Thr Glu Gln 1 5 10 15 Ile Leu Ala Ser Gly Ser Arg Asp Tyr ThrLeu Lys Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:119: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CSTF 50kDa rIII, Fig. 20 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:119: Ala His Asp Gly Ala Glu Val Cys Ser Ala Ile Phe Ser LysAsn Ser 1 5 10 15 Lys Tyr Ile Leu Ser Ser Gly Lys Asp Ser Val Ala LysLeu Trp Glu 20 25 30 (2) INFORMATION FOR SEQ ID NO:120: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: CSTF50kDa rIV, Fig. 20 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:120: Val His ArgThr Gln Ala Val Phe Asn His Thr Glu Asp Tyr Val Leu 1 5 10 15 Leu ProAsp Glu Arg Thr Ile Ser Leu Cys Cys Trp Asp 20 25 (2) INFORMATION FORSEQ ID NO:121: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: CSTF 50kDa rV, Fig. 20 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:121: Gly His Asn Asn Ile Val Arg Cys Ile Val His Ser Pro ThrAsn Pro 1 5 10 15 Gly Phe Met Thr Cys Ser Asp Asp Phe Arg Ala Arg PheTrp Tyr 20 25 30 (2) INFORMATION FOR SEQ ID NO:122: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-BETA DROSOPH rI, Fig. 23 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:122: GlyHis Leu Ala Lys Ile Tyr Ala Met His Trp Gly Asn Asp Ser Arg 1 5 10 15Asn Leu Val Ser Ala Ser Gln Asp Gly Lys Leu Ile Val Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:123: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: G- BETA DROSOPH rII, Fig. 23 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:123: Gly His Gly Gly Tyr Leu Ser Cys CysArg Phe Leu Asp Asp Asn Gln 1 5 10 15 Ile Val Thr Ser Ser Gly Asp MetSer Cys Gly Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:124: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G- BETA DROSOPH rIII, Fig. 23 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:124: Gly His Thr Gly Asp Val Met Ala Leu Ser LeuAla Pro Gln Cys Lys 1 5 10 15 Thr Phe Val Ser Gly Ala Cys Asp Ala SerAla Lys Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:125: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G- BETA DROSOPH rIV, Fig. 23 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:125: Gly His Glu Ser Asp Ile Asn Ala Val Thr PhePhe Pro Asn Gly Gln 1 5 10 15 Ala Phe Ala Thr Gly Ser Asp Asp Ala ThrCys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:126: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G- BETA DROSOPH rV, Fig. 23 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:126: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ala Phe Ser Lys 1 5 10 15 Ser Gly Arg Leu Leu Leu Ala Gly Tyr AspAsp Phe Asn Cys Asn Val 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:127: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G- BETA DROSOPH rVI, Fig. 23 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:127: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Glu Asn Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp Ser PheLeu Arg Val Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:128: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-BETA HUMAN rI, Fig. 24 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:128: Gly His Asn Gly Trp Val Thr Gln Ile Ala Thr Thr Pro GlnPhe Pro 1 5 10 15 Asp Met Ile Leu Ser Ala Ser Arg Asp Lys Thr Ile IleMet Trp Lys 20 25 30 (2) INFORMATION FOR SEQ ID NO:129: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-BETAHUMAN rII, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:129: Gly His SerHis Phe Val Ser Asp Val Val Ile Ser Ser Asp Gly Gln 1 5 10 15 Phe AlaLeu Ser Gly Ser Trp Asp Gly Thr Leu Arg Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:130: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: G-BETA HUMAN rIII, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:130: Gly His Thr Lys Asp Val Leu Ser Val Ala PheSer Ser Asp Asn Arg 1 5 10 15 Gln Ile Val Ser Gly Ser Arg Asp Lys ThrIle Lys Leu Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:131: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-BETA HUMAN rIV, Fig. 24 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:131: Ser His Ser Glu Trp Val Ser Cys Val Arg Phe Ser Pro AsnSer Ser 1 5 10 15 Asn Pro Ile Ile Val Ser Cys Gly Trp Asp Lys Leu ValLys Val Trp 20 25 30 Asn (2) INFORMATION FOR SEQ ID NO:132: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-BETAHUMAN rV, Fig. 24 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:132: Gly His ThrGly Tyr Leu Asn Thr Val Thr Val Ser Pro Asp Gly Ser 1 5 10 15 Leu CysAla Ser Gly Gly Lys Asp Gly Gln Ala Met Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:133: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:36 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: G-BETA HUMAN rVI, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:133: Lys His Leu Tyr Thr Leu Asp Gly Gly Asp IleIle Asn Ala Leu Cys 1 5 10 15 Phe Ser Pro Asn Arg Tyr Trp Leu Cys AlaAla Thr Gly Pro Ser Ile 20 25 30 Lys Ile Trp Asp 35 (2) INFORMATION FORSEQ ID NO:134: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-BETA HUMAN rVII, Fig. 24 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:134: Ala Glu Pro Pro Gln Cys Thr Ser Leu Ala TrpSer Ala Asp Gly Gln 1 5 10 15 Thr Leu Phe Ala Gly Tyr Thr Asp Asn LeuVal Arg Val Trp Gln 20 25 30 (2) INFORMATION FOR SEQ ID NO:135: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta 1 bovine rI, Fig. 21 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:135: Gly His Leu Ala Lys Ile Tyr Ala Met His TrpGly Thr Asp Ser Arg 1 5 10 15 Leu Leu Val Ser Ala Ser Gln Asp Gly LysLeu Ile Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:136: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta 1 bovine rII, Fig. 21 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:136: Gly His Thr Gly Tyr Leu Ser Cys Cys Arg PheLeu Asp Asp Asn Gln 1 5 10 15 Ile Val Thr Ser Ser Gly Asp Thr Thr CysAla Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:137: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta1 bovine rIII, Fig. 21 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:137: Gly HisThr Gly Asp Val Met Ser Leu Ser Leu Ala Pro Asp Thr Arg 1 5 10 15 LeuPhe Val Ser Gly Ala Cys Asp Ala Ser Ala Lys Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:138: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: G-Beta 1 bovine rIV, Fig. 21 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:138: Gly His Glu Ser Asp Ile Asn Ala IleCys Phe Phe Pro Asn Gly Asn 1 5 10 15 Ala Phe Ala Thr Gly Ser Asp AspAla Thr Cys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:139:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta 1 bovine rV, Fig. 21 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:139: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ser Phe Ser Lys 1 5 10 15 Ser Gly Arg Leu Leu Leu Ala Gly Tyr AspAsp Phe Asn Cys Asn Val 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:140: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta 1 bovine rVI, Fig. 21 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:140: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Asp Asp Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp Ser PheLeu Lys Ile Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:141: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta-bovine(2) rI, Fig. 22 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:141: Gly His Leu Ala Lys Ile Tyr Ala Met His TrpGly Thr Asp Ser Arg 1 5 10 15 Leu Leu Val Ser Ala Ser Gln Asp Gly LysLeu Ile Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:142: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta-bovine(2) rII, Fig. 22 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:142: Gly His Thr Gly Tyr Leu Ser Cys Cys Arg PheLeu Asp Asp Asn Gln 1 5 10 15 Ile Ile Thr Ser Ser Gly Asp Thr Thr CysAla Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:143: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:G-Beta-bovine(2) rIII, Fig. 22 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:143:Gly His Ser Gly Asp Val Met Ser Leu Ser Leu Ala Pro Asp Gly Arg 1 5 1015 Thr Phe Val Ser Gly Ala Cys Asp Ala Ser Ile Lys Leu Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:144: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta-bovine(2) rIV, Fig. 22(xi) SEQUENCE DESCRIPTION: SEQ ID NO:144: Gly His Glu Ser Asp Ile AsnAla Val Ala Phe Phe Pro Asn Gly Tyr 1 5 10 15 Ala Phe Thr Thr Gly SerAsp Asp Ala Thr Cys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ IDNO:145: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta-bovine(2) rV, Fig. 22 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:145: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ala Phe Ser Arg 1 5 10 15 Ser Gly Arg Leu Leu Leu Ala Gly Tyr AspAsp Phe Asn Cys Asn Ile 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:146: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta-bovine(2) rVI, Fig. 22 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:146: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Asp Asp Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp Ser PheLeu Lys Ile Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:147: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta2(Human) rI, Fig. 25 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:147: Gly His Leu Ala Lys Ile Tyr Ala Met His TrpGly Thr Asp Ser Arg 1 5 10 15 Leu Leu Val Ser Ala Ser Gln Asp Gly LysLeu Ile Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:148: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta2(Human) rII, Fig. 25 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:148: Gly His Thr Gly Tyr Leu Ser Cys Cys Arg PheLeu Asp Asp Asn Gln 1 5 10 15 Ile Ile Thr Ser Ser Gly Asp Thr Thr CysAla Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:149: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:G-Beta2(Human) rIII, Fig. 25 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:149:Gly His Ser Gly Asp Val Met Ser Leu Ser Leu Ala Pro Asp Gly Arg 1 5 1015 Thr Phe Val Ser Gly Ala Cys Asp Ala Ser Ile Lys Leu Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:150: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta2(Human) rIV, Fig. 25(xi) SEQUENCE DESCRIPTION: SEQ ID NO:150: Gly His Glu Ser Asp Ile AsnAla Val Ala Phe Phe Pro Asn Gly Tyr 1 5 10 15 Ala Phe Thr Thr Gly SerAsp Asp Ala Thr Cys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ IDNO:151: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta2(Human) rV, Fig. 25 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:151: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ala Phe Ser Arg 1 5 10 15 Ser Gly Arg Leu Leu Leu Ala Gly Tyr AspAsp Phe Asn Cys Asn Ile 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:152: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta2(Human) rVI, Fig. 25 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:152: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Asp Asp Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp Ser PheLeu Lys Ile Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:153: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta4(mouse) rI, Fig. 26 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:153: Gly His Leu Ala Lys Ile Tyr Ala Met His TrpGly Tyr Asp Ser Arg 1 5 10 15 Leu Leu Val Ser Ala Ser Gln Asp Gly LysLeu Ile Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:154: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta4(mouse) rII, Fig. 26 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:154: Gly His Thr Gly Tyr Leu Ser Cys Cys Arg PheLeu Asp Asp Gly Gln 1 5 10 15 Ile Ile Thr Ser Ser Gly Asp Thr Thr CysAla Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:155: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:G-Beta4(mouse) rIII, Fig. 26 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:155:Gly His Ser Gly Asp Val Met Ser Leu Ser Leu Ser Pro Asp Leu Lys 1 5 1015 Thr Phe Val Ser Gly Ala Cys Asp Ala Ser Ser Lys Leu Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:156: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: G-Beta4(mouse) rIV, Fig. 26(xi) SEQUENCE DESCRIPTION: SEQ ID NO:156: Gly His Ile Ser Asp Ile AsnAla Val Ser Phe Phe Pro Ser Gly Tyr 1 5 10 15 Ala Phe Ala Thr Gly SerAsp Asp Ala Thr Cys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FOR SEQ IDNO:157: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta4(mouse) rV, Fig. 26 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:157: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ala Phe Ser Lys 1 5 10 15 Ser Gly Arg Leu Leu Leu Ala Gly Tyr AspAsp Phe Asn Cys Ser Val 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:158: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: G-Beta4(mouse) rVI, Fig. 26 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:158: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Asp Asp Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp Ser PheLeu Arg Ile Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:159: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GROUCHO PROT. DRSPH rI, Fig. 27 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:159: Thr Ser Ala Ala Pro Ala Cys Tyr Ala Leu AlaSer Pro Asp Ser Lys 1 5 10 15 Val Cys Phe Ser Cys Cys Ser Asp Gly AsnIle Ala Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:160: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GROUCHO PROT. DRSPH rII, Fig. 27 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:160: Gly His Thr Asp Gly Ala Ser Cys Ile Asp IleSer Pro Asp Gly Ser 1 5 10 15 Arg Leu Trp Thr Gly Gly Leu Asp Asn ThrVal Arg Ser Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:161: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GTP binding prt squid rI, Fig. 28 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:161: Gly His Leu Ala Lys Ile Tyr Ala Met His TrpAla Ser Asp Ser Arg 1 5 10 15 Asn Leu Val Ser Ala Ser Gln Asp Gly LysLeu Ile Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:162: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GTP binding prt squid rII, Fig. 28 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:162: Gly His Thr Gly Tyr Leu Ser Cys Cys Arg PheIle Asp Asp Asn Gln 1 5 10 15 Ile Val Thr Ser Ser Gly Asp Met Thr CysAla Leu Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:163: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GTPbinding prt squid rIII, Fig. 28 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:163: Gly His Thr Gly Asp Val Met Ser Leu Ser Leu Ala Pro Asp Met Arg1 5 10 15 Thr Phe Val Ser Gly Ala Cys Asp Ala Ser Ala Lys Leu Phe Asp 2025 30 (2) INFORMATION FOR SEQ ID NO:164: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: GTP binding prt squid rIV,Fig. 28 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:164: Gly His Glu Ser AspIle Asn Ala Ile Thr Tyr Phe Pro Asn Gly Phe 1 5 10 15 Ala Phe Ala ThrGly Ser Asp Asp Ala Thr Cys Arg Leu Phe Asp 20 25 30 (2) INFORMATION FORSEQ ID NO:165: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GTP binding prt squid rV, Fig. 28 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:165: Ser His Asp Asn Ile Ile Cys Gly Ile Thr SerVal Ala Phe Ser Lys 1 5 10 15 Ser Gly Arg Leu Leu Leu Gly Gly Tyr AspAsp Phe Asn Cys Asn Val 20 25 30 Trp Asp (2) INFORMATION FOR SEQ IDNO:166: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: GTP binding prt squid rVI, Fig. 28 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:166: Gly His Asp Asn Arg Val Ser Cys Leu Gly ValThr Glu Asp Gly Met 1 5 10 15 Ala Val Ala Thr Gly Ser Trp Asp 20 (2)INFORMATION FOR SEQ ID NO:167: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: IEF SSP 9306 rI, Fig. 29 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:167: Gly His Gln Lys Glu Gly Tyr Gly Leu Ser TrpAsn Pro Asn Leu Ser 1 5 10 15 Gly His Leu Leu Ser Ala Ser Asp Asp HisThr Ile Cys Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:168: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: IEF SSP 9306 rII, Fig. 29 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:168: Gly His Thr Ala Val Val Glu Asp Val Ser Trp His Leu LeuHis Glu 1 5 10 15 Ser Leu Phe Gly Ser Val Ala Asp Asp Gln Lys Leu MetIle Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:169: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 37 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: IEFSSP 9306 rIII, Fig. 29 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:169: Ser HisSer Val Asp Ala His Thr Ala Glu Val Asn Cys Leu Ser Phe 1 5 10 15 AsnPro Tyr Ser Glu Phe Ile Leu Ala Thr Gly Ser Ala Asp Lys Thr 20 25 30 ValAla Leu Trp Asp 35 (2) INFORMATION FOR SEQ ID NO:170: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 37 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: IEFSSP 9306 rIV, Fig. 29 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:170: Leu HisSer Phe Glu Ser His Lys Asp Glu Ile Phe Gln Val Gln Trp 1 5 10 15 SerPro His Asn Glu Thr Ile Leu Ala Ser Ser Gly Thr Asp Arg Arg 20 25 30 LeuAsn Val Trp Asp 35 (2) INFORMATION FOR SEQ ID NO:171: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: IEFSSP 9306 rV, Fig. 29 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:171: Ile GlyGlu Glu Gln Ser Pro Glu Asp Ala Glu Asp Gly Pro Pro Glu 1 5 10 15 LeuLeu Phe Ile His Gly Gly His Thr Ala Lys Ile Ser Asp Phe Ser 20 25 30 TrpAsn (2) INFORMATION FOR SEQ ID NO:172: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: HUMAN 12.3 rI, Fig. 30 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:172: Gly His Asn Gly Trp Val Thr Gln IleAla Thr Thr Pro Gln Phe Pro 1 5 10 15 Asp Met Ile Leu Ser Ala Ser ArgAsp Lys Thr Ile Ile Met Trp Lys 20 25 30 (2) INFORMATION FOR SEQ IDNO:173: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: HUMAN 12.3 rII, Fig. 30 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:173: Gly His Ser His Phe Val Ser Asp Val Val Ile Ser Ser AspGly Gln 1 5 10 15 Phe Ala Leu Ser Gly Ser Trp Asp Gly Thr Leu Arg LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:174: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: HUMAN12.3 rIII, Fig. 30 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:174: Gly His ThrLys Asp Val Leu Ser Val Ala Phe Ser Ser Asp Asn Arg 1 5 10 15 Gln IleVal Ser Gly Ser Arg Asp Lys Thr Ile Lys Leu Trp Asn 20 25 30 (2)INFORMATION FOR SEQ ID NO:175: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: HUMAN 12.3 rIV, Fig. 30 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:175: Ser His Ser Glu Trp Val Ser Cys Val Arg PheSer Pro Asn Ser Ser 1 5 10 15 Asn Pro Ile Ile Val Ser Cys Gly Trp AspLys Leu Val Lys Val Trp 20 25 30 Asn (2) INFORMATION FOR SEQ ID NO:176:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: HUMAN 12.3 rV, Fig. 30 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:176: Gly His Thr Gly Tyr Leu Asn Thr Val Thr Val Ser Pro AspGly Ser 1 5 10 15 Leu Cys Ala Ser Gly Gly Lys Asp Gly Gln Ala Met LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:177: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 36 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: HUMAN12.3 rVI, Fig. 30 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:177: Lys His LeuTyr Thr Leu Asp Gly Gly Asp Ile Ile Asn Ala Leu Cys 1 5 10 15 Phe SerPro Asn Arg Tyr Trp Leu Cys Ala Ala Thr Gly Pro Ser Ile 20 25 30 Lys IleTrp Asp 35 (2) INFORMATION FOR SEQ ID NO:178: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 38 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: HUMAN12.3 rVII, Fig. 30 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:178: Val Ile SerThr Ser Ser Lys Ala Glu Pro Pro Gln Cys Thr Ser Leu 1 5 10 15 Ala TrpSer Ala Asp Gly Gln Thr Leu Phe Ala Gly Tyr Thr Asp Asn 20 25 30 Leu ValArg Val Trp Gln 35 (2) INFORMATION FOR SEQ ID NO:179: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:IEF-7442-human rI, Fig. 31 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:179: GlyHis Gln Lys Glu Gly Tyr Gly Leu Ser Trp Asn Ser Asn Leu Ser 1 5 10 15Gly His Leu Leu Ser Ala Ser Asp Asp His Thr Val Cys Leu Trp Asp 20 25 30(2) INFORMATION FOR SEQ ID NO:180: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: IEF-7442-human rII, Fig. 31(xi) SEQUENCE DESCRIPTION: SEQ ID NO:180: Gly His Ser Ala Val Val GluAsp Val Ala Trp His Leu Leu His Glu 1 5 10 15 Ser Leu Phe Gly Ser ValAla Asp Asp Gln Lys Leu Met Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQID NO:181: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: IEF-7442-human rIII, Fig. 31 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:181: Ala His Thr Ala Glu Val Asn Cys Leu Ser PheAsn Pro Tyr Ser Glu 1 5 10 15 Phe Ile Leu Ala Thr Gly Ser Ala Asp LysThr Val Ala Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:182: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 24 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: IEF-7442-human rIV, Fig. 31 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:182: Val His Trp Ser Pro His Asn Glu Thr Ile LeuAla Ser Ser Gly Thr 1 5 10 15 Asp Arg Arg Leu Asn Val Trp Asp 20 (2)INFORMATION FOR SEQ ID NO:183: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: IEF-7442-human rV, Fig. 31 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:183: Gly His Thr Ala Lys Ile Ser Asp Phe Ser TrpAsn Pro Asn Glu Pro 1 5 10 15 Trp Val Ile Cys Ser Val Ser Glu Asp AsnIle Met Gln Ile Trp Gln 20 25 30 (2) INFORMATION FOR SEQ ID NO:184: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Insulin-like GF binding protein complex rI, Fig. 32(xi) SEQUENCE DESCRIPTION: SEQ ID NO:184: Ala His Thr Pro Ala Leu AlaSer Leu Gly Leu Ser Asn Asn Arg Leu 1 5 10 15 Ser Arg Leu Glu Asp GlyLeu Phe Glu Gly Leu Gly Ser Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQID NO:185: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Insulin-like growth factor bind. pro. complex-ratrI, Fig. 33 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:185: Thr His Thr ProSer Leu Ala Ser Leu Ser Leu Ser Ser Asn Leu Leu 1 5 10 15 Gly Arg LeuGlu Glu Gly Leu Phe Gln Gly Leu Ser His Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:186: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:47 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: Insulin-like growth factor bind. pro.complex-rat rII, Fig. 33 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:186: AsnHis Leu Glu Thr Leu Ala Glu Gly Leu Phe Ser Ser Leu Gly Arg 1 5 10 15Val Arg Tyr Leu Ser Leu Arg Asn Asn Ser Leu Gln Thr Phe Ser Pro 20 25 30Gln Pro Gly Leu Glu Arg Leu Trp Leu Asp Ala Asn Pro Trp Asp 35 40 45 (2)INFORMATION FOR SEQ ID NO:187: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: LIS1 (human) rI, Fig. 34 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:187: Gly His Arg Ser Pro Val Thr Arg Val Ile PheHis Pro Val Phe Ser 1 5 10 15 Val Met Val Ser Ala Ser Glu Asp Ala ThrIle Lys Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:188: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: LIS1 (human) rII, Fig. 34 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:188: Gly His Thr Asp Ser Val Gln Asp Ile Ser Phe Asp His SerGly Lys 1 5 10 15 Leu Leu Ala Ser Cys Ser Ala Asp Met Thr Ile Lys LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:189: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: LIS1(human) rIII, Fig. 34 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:189: Gly HisAsp His Asn Val Ser Ser Val Ala Ile Met Pro Asn Gly Asp 1 5 10 15 HisIle Val Ser Ala Ser Arg Asp Lys Thr Ile Lys Met Trp Glu 20 25 30 (2)INFORMATION FOR SEQ ID NO:190: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: LIS1 (human) rIV, Fig. 34 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:190: Gly His Arg Glu Trp Val Arg Met Val Arg ProAsn Gln Asp Gly Thr 1 5 10 15 Leu Ile Ala Ser Cys Ser Asn Asp Gln ThrVal Arg Val Trp Val 20 25 30 (2) INFORMATION FOR SEQ ID NO:191: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: LIS1 (human) rV, Fig. 34 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:191: Gly Ser Glu Thr Lys Lys Ser Gly Lys Pro Gly Pro Phe LeuLeu Ser 1 5 10 15 Gly Ser Arg Asp Lys Thr Lys Met Trp Asp 20 25 (2)INFORMATION FOR SEQ ID NO:192: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: LIS1 (human) rVI, Fig. 34 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:192: Gly His Asp Asn Trp Val Arg Gly Val Leu PheHis Ser Gly Gly Lys 1 5 10 15 Phe Ile Leu Ser Cys Ala Asp Asp Lys ThrLeu Arg Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:193: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: LIS1 (human) rVII, Fig. 34 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:193: Ala His Glu His Phe Val Thr Ser Leu Asp PheHis Lys Thr Ala Pro 1 5 10 15 Tyr Val Val Thr Gly Ser Val Asp Gln ThrVal Lys Val Trp Glu 20 25 30 (2) INFORMATION FOR SEQ ID NO:194: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: MD6 rI, Fig. 35 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:194: Gly His Ser Ala Arg Val Tyr Ala Leu Tyr Tyr Lys Asp Gly Leu Leu1 5 10 15 Cys Thr Gly Ser Asp Asp Leu Ser Ala Lys Leu Trp Asp 20 25 (2)INFORMATION FOR SEQ ID NO:195: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:27 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: MD6 rII, Fig. 35 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:195: Thr His Thr Cys Ala Ala Val Lys Phe Asp GluGln Lys Leu Val Thr 1 5 10 15 Gly Ser Phe Asp Asn Thr Val Ala Cys TrpGlu 20 25 (2) INFORMATION FOR SEQ ID NO:196: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: MD6rIII, Fig. 35 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:196: Gly His Thr GlyAla Val Phe Ser Val Asp Tyr Ser Asp Glu Leu Asp 1 5 10 15 Ile Leu ValSer Gly Ser Ala Asp Phe Ala Val Lys Val Trp Ala 20 25 30 (2) INFORMATIONFOR SEQ ID NO:197: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 40 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: MD6 rIV, Fig. 35 (xi) SEQUENCE DESCRIPTION: SEQID NO:197: Gly His Thr Glu Trp Val Thr Lys Val Val Leu Gln Lys Cys LysVal 1 5 10 15 Lys Ser Leu Leu His Ser Pro Gly Asp Tyr Ile Leu Leu SerAla Asp 20 25 30 Lys Tyr Glu Ile Lys Ile Trp Pro 35 40 (2) INFORMATIONFOR SEQ ID NO:198: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: MSL1 rI, Fig. 36 (xi) SEQUENCE DESCRIPTION: SEQID NO:198: Lys His Asp Gly Gly Val Asn Ser Cys Arg Phe Asn Tyr Lys AsnSer 1 5 10 15 Leu Ile Leu Ala Ser Ala Asp Ser Asn Gly Arg Leu Asn LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:199: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: MSL1rII, Fig. 36 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:199: Glu His Gly ThrSer Val Ser Thr Leu Glu Trp Ser Pro Asn Phe Asp 1 5 10 15 Thr Val LeuAla Thr Ala Gly Gln Glu Asp Gly Leu Val Lys Leu Trp 20 25 30 Asp (2)INFORMATION FOR SEQ ID NO:200: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: MSL1 rIII, Fig. 36 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:200: Gly His Met Leu Gly Val Asn Asp Ile Ser TrpAsp Ala His Asp Pro 1 5 10 15 Trp Leu Met Cys Ser Val Ala Asn Asp AsnSer Val His Ile Trp Lys 20 25 30 (2) INFORMATION FOR SEQ ID NO:201: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: MUS MUSCULUS PROTEIN rI, Fig. 37 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:201: Gly His Ser Gly Cys Val Asn Thr Val His PheAsn Gln His Gly Thr 1 5 10 15 Leu Leu Ala Ser Gly Ser Asp Asp Leu LysVal Ile Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:202: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: MUS MUSCULUS PROTEIN rII, Fig. 37 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:202: Gly His Ile Phe Ile Trp Glu Lys Ser Ser CysGln Ile Val Gln Phe 1 5 10 15 Leu Glu Ala Asp Glu Gly Gly Thr Ile AsnCys Ile Asp Ser His Pro 20 25 30 Tyr Leu Pro Val Leu Ala Ser Ser Gly LeuAsp His Glu Val Lys Ile 35 40 45 Trp Ser 50 (2) INFORMATION FOR SEQ IDNO:203: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: ORF RB1 rI, Fig. 38 (xi) SEQUENCE DESCRIPTION: SEQID NO:203: Lys His Asp Gly Gly Val Asn Ser Cys Arg Phe Asn Tyr Lys AsnSer 1 5 10 15 Leu Ile Leu Ala Ser Ala Asp Ser Asn Gly Arg Leu Asn LeuTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:204: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: ORFRB1 rII, Fig. 38 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:204: Glu His GlyThr Ser Val Ser Thr Leu Glu Trp Ser Pro Asn Phe Asp 1 5 10 15 Thr ValLeu Ala Thr Ala Gly Gln Glu Asp Gly Leu Val Lys Leu Trp 20 25 30 Asp (2)INFORMATION FOR SEQ ID NO:205: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: ORF RB1 rIII, Fig. 38 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:205: Gly His Met Leu Gly Val Asn Asp Ile Ser TrpAsp Ala His Asp Pro 1 5 10 15 Trp Leu Met Cys Ser Val Ala Asn Asp AsnSer Val His Ile Trp Lys 20 25 30 (2) INFORMATION FOR SEQ ID NO:206: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: Periodic Trp prt rI, Fig. 39 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:206: Gly His Ile Thr Thr His His Thr Asp Ala ValLeu Ser Met Ala His 1 5 10 15 Asn Lys Tyr Phe Arg Ser Val Leu Ala SerThr Ser Ala Asp His Thr 20 25 30 Val Lys Leu Trp Asp 35 (2) INFORMATIONFOR SEQ ID NO:207: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 47 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: Periodic Trp prt rII, Fig. 39 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:207: Ile His Ser Asn Lys Asn Val Ser Ser Ser GluTrp His Met Leu Asn 1 5 10 15 Gly Ser Ile Leu Leu Thr Gly Gly Tyr AspSer Arg Val Ala Leu Thr 20 25 30 Asp Val Arg Ile Ser Asp Glu Ser Gln MetSer Lys Tyr Trp Ser 35 40 45 (2) INFORMATION FOR SEQ ID NO:208: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: PLAP rI, Fig. 40 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:208: Gly His Lys Asp Thr Val Cys Ser Leu Ser Ser Gly Lys Phe Gly Thr1 5 10 15 Leu Leu Ser Gly Ser Trp Asp Thr Thr Ala Lys Val Trp Leu 20 2530 (2) INFORMATION FOR SEQ ID NO:209: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: PLAP rII, Fig. 40 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:209: Gly His Thr Ala Ala Val Trp Ala Val Lys IleLeu Pro Glu Gln Gly 1 5 10 15 Leu Met Leu Thr Gly Ser Ala Asp Lys ThrIle Lys Leu Trp Lys 20 25 30 (2) INFORMATION FOR SEQ ID NO:210: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: PLAP rIII, Fig. 40 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:210: Gly His Glu Asp Cys Val Arg Gly Leu Ala Ile Leu Ser Glu Thr Glu1 5 10 15 Phe Leu Ser Cys Ala Asn Asp Ala Ser Ile Arg Arg Trp Gln 20 2530 (2) INFORMATION FOR SEQ ID NO:211: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: PLAP rIV, Fig. 40 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:211: Gly His Thr Asn Tyr Ile Tyr Ser Ile Ser ValPhe Pro Asn Ser Lys 1 5 10 15 Asp Phe Val Thr Thr Ala Glu Asp Arg SerLeu Arg Ile Trp Lys 20 25 30 (2) INFORMATION FOR SEQ ID NO:212: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDING PROTEIN - HUMAN. rI, Fig. 41(xi) SEQUENCE DESCRIPTION: SEQ ID NO:212: Gly His Gln Lys Glu Gly TyrGly Leu Ser Trp Asn Pro Asn Leu Ser 1 5 10 15 Gly His Leu Leu Ser AlaSer Asp Asp His Thr Ile Cys Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQID NO:213: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDING PROTEIN - HUMAN rII, Fig. 41(xi) SEQUENCE DESCRIPTION: SEQ ID NO:213: Gly His Thr Ala Val Val GluAsp Val Ser Trp His Leu Leu His Glu 1 5 10 15 Ser Leu Phe Gly Ser ValAla Asp Asp Gln Lys Leu Met Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQID NO:214: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDING PROTEIN - HUMAN rIII, Fig. 41(xi) SEQUENCE DESCRIPTION: SEQ ID NO:214: Ser His Ser Val Asp Ala HisThr Ala Glu Val Asn Cys Leu Ser Phe 1 5 10 15 Asn Pro Tyr Ser Glu PheIle Leu Ala Thr Gly Ser Ala Asp Lys Thr 20 25 30 Val Ala Leu Trp Asp 35(2) INFORMATION FOR SEQ ID NO:215: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDINGPROTEIN - HUMAN rIV, Fig. 41 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:215:Ser His Lys Asp Glu Ile Phe Gln Val Gln Trp Ser Pro His Asn Glu 1 5 1015 Thr Ile Leu Ala Ser Ser Gly Thr Asp Arg Arg Leu Asn Val Trp Asp 20 2530 (2) INFORMATION FOR SEQ ID NO:216: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: RETINOBLASTOMA BINDINGPROTEIN - HUMAN rV, Fig. 41 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:216:Gly His Thr Ala Lys Ile Ser Asp Phe Ser Trp Asn Pro Asn Glu Pro 1 5 1015 Trp Val Ile Cys Ser Val Ser Glu Asp Asn Ile Met Gln Val Trp Gln 20 2530 (2) INFORMATION FOR SEQ ID NO:217: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: S253 PROTEIN rI, Fig. 42 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:217: Glu His Ala Leu Asp Ile Leu Asp AlaAsn Trp Ser Lys Asn Gly Phe 1 5 10 15 Leu Ile Thr Ala Ser Met Asp LysThr Ala Lys Leu Trp His 20 25 30 (2) INFORMATION FOR SEQ ID NO:218: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: S253 PROTEIN rII, Fig. 42 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:218: Val His Pro Asp Phe Val Thr Ser Ala Ile Phe Phe Pro AsnAsp Asp 1 5 10 15 Arg Phe Ile Ile Thr Gly Cys Leu Asp His Arg Cys ArgLeu Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:219: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: SOF1rI, Fig. 43 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:219: Gly His Arg AspGly Val Tyr Ala Ile Ala Lys Asn Tyr Gly Ser Leu 1 5 10 15 Asn Lys LeuAla Thr Gly Ser Ala Asp Gly Val Ile Lys Tyr Trp 20 25 30 (2) INFORMATIONFOR SEQ ID NO:220: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: SOF1 rII, Fig. 43 (xi) SEQUENCE DESCRIPTION: SEQID NO:220: Gly Leu Cys Val Thr Gln Pro Arg Phe His Asp Lys Lys Pro AspLeu 1 5 10 15 Lys Ser Gln Asn Phe Met Leu Ser Cys Ser Asp Asp Lys ThrVal Lys 20 25 30 Leu Trp Ser 35 (2) INFORMATION FOR SEQ ID NO:221: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: SOF1 rIII, Fig. 43 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:221: Gly Leu Ile Arg Thr Phe Asp Gly Glu Ser Ala Phe Gln Gly Ile Asp1 5 10 15 Ser His Arg Glu Asn Ser Thr Phe Ala Thr Gly Gly Ala Lys IleHis 20 25 30 Leu Trp Asp 35 (2) INFORMATION FOR SEQ ID NO:222: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 39 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: SOF1 rIV, Fig. 43 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:222: Gly His Ser Arg Glu Ile Tyr His Thr Lys Arg Met Gln His Val Phe1 5 10 15 Val Lys Tyr Ser Met Asp Ser Lys Tyr Ile Ile Ser Gly Ser AspAsp 20 25 30 Gly Asn Val Arg Leu Trp Arg 35 (2) INFORMATION FOR SEQ IDNO:223: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: STE4-YEAST rI, Fig. 44 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:223: Gly His Asn Asn Lys Ile Ser Asp Phe Arg Trp Ser Arg AspSer Lys 1 5 10 15 Arg Ile Leu Ser Ala Ser Gln Asp Gly Phe Met Leu IleTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:224: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:STE4-YEAST rII, Fig. 44 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:224: GlyHis Thr Cys Tyr Ile Ser Asp Ile Glu Phe Thr Asp Asn Ala His 1 5 10 15Ile Leu Thr Ala Ser Gly Asp Met Thr Cys Ala Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:225: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:37 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: STE4-YEAST rIII, Fig. 44 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:225: Asp His Leu Gly Asp Val Leu Ala Leu Ala IlePro Glu Glu Pro Asn 1 5 10 15 Leu Glu Asn Ser Ser Asn Thr Phe Ala SerCys Gly Ser Asp Gly Tyr 20 25 30 Thr Tyr Ile Trp Asp 35 (2) INFORMATIONFOR SEQ ID NO:226: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 aminoacids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE:(C) INDIVIDUAL ISOLATE: STE4-YEAST rIV, Fig. 44 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:226: Leu Asp Asn Gln Gly Val Val Ser Leu Asp PheSer Ala Ser Gly Arg 1 5 10 15 Leu Met Tyr Ser Cys Tyr Thr Asp Ile GlyCys Val Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:227: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: STE4-YEAST rV, Fig. 44 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:227: Gly His Gly Gly Arg Val Thr Gly Val Arg Ser Ser Pro AspGly Leu 1 5 10 15 Ala Val Cys Thr Gly Ser Trp Asp Ser Thr Met Lys IleTrp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:228: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE:TRNSCRPTION FCTR TIIF rI, Fig. 45 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:228: Gly His Thr Gly Pro Val Tyr Arg Cys Ala Phe Ala Pro Glu Met Asn1 5 10 15 Leu Leu Leu Ser Cys Ser Glu Asp Ser Thr Ile Arg Leu Trp Ser 2025 30 (2) INFORMATION FOR SEQ ID NO:229: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TRNSCRPTION FCTR TIIF rII,Fig. 45 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:229: Gly His Val Tyr ProVal Trp Asp Val Arg Phe Ala Pro His Gly Tyr 1 5 10 15 Tyr Phe Val SerCys Ser Tyr Asp Lys Thr Ala Arg Leu Trp Ala 20 25 30 (2) INFORMATION FORSEQ ID NO:230: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids(B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide(iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TRNSCRPTION FCTR TIIF rIII, Fig. 45 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:230: Gly His Leu Ser Asp Val Asp Cys Val Gln PheHis Pro Asn Ser Asn 1 5 10 15 Tyr Val Ala Thr Gly Ser Ser Asp Arg ThrVal Arg Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:231: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TRNSCRPTION FCTR TIIF rIV, Fig. 45 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:231: Gly His Lys Gly Ser Val Ser Ser Leu Ala PheSer Ala Cys Gly Arg 1 5 10 15 Tyr Leu Ala Ser Gly Ser Val Asp His AsnIle Ile Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:232: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TRNSCRPTION FCTR TIIF rV, Fig. 45 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:232: Arg His Thr Ser Thr Val Thr Thr Ile Thr PheSer Arg Asp Gly Thr 1 5 10 15 Val Leu Ala Ala Ala Gly Leu Asp Asn AsnLeu Thr Leu Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:233: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 rI, Fig. 46 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:233: Ser Ser Asp Leu Tyr Ile Arg Ser Val Cys Phe Ser Pro Asp Gly Lys1 5 10 15 Phe Leu Ala Thr Gly Ala Glu Asp Arg Leu Ile Arg Ile Trp Asp 2025 30 (2) INFORMATION FOR SEQ ID NO:234: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1 rII, Fig. 46 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:234: Gly His Glu Gln Asp Ile Tyr Ser LeuAsp Tyr Phe Pro Ser Gly Asp 1 5 10 15 Lys Leu Val Ser Gly Ser Gly AspArg Thr Val Arg Ile Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:235:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 rIII, Fig. 46 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:235: Ile Glu Asp Gly Val Thr Thr Val Ala Val Ser Pro Gly Asp Gly Lys1 5 10 15 Tyr Ile Ala Ala Gly Ser Leu Asp Arg Ala Val Arg Val Trp Asp 2025 30 (2) INFORMATION FOR SEQ ID NO:236: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1 rIV, Fig. 46 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:236: Gly His Lys Asp Ser Val Tyr Ser ValVal Phe Thr Arg Asp Gly Gln 1 5 10 15 Ser Val Val Ser Gly Ser Leu AspArg Ser Val Lys Leu Trp Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:237:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 rV, Fig. 46 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:237: Gly His Lys Asp Phe Val Leu Ser Val Ala Thr Thr Gln Asn Asp Glu1 5 10 15 Tyr Ile Leu Ser Gly Ser Lys Asp Arg Gly Val Leu Phe Trp Asp 2025 30 (2) INFORMATION FOR SEQ ID NO:238: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 22 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1 HOMOLOG rI, Fig. 47(xi) SEQUENCE DESCRIPTION: SEQ ID NO:238: Asp Phe Ser Asp Asp Cys ArgIle Ala Ala Ala Gly Phe Gln Asp Ser 1 5 10 15 Tyr Ile Lys Ile Trp Ser 20(2) INFORMATION FOR SEQ ID NO:239: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1 HOMOLOG rII, Fig. 47 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:239: Gly His Ser Gly Thr Val Tyr Ser ThrSer Phe Ser Pro Asp Asn Lys 1 5 10 15 Tyr Leu Leu Ser Gly Ser Glu AspLys Thr Val Arg Leu Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:240:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 HOMOLOG rIII, Fig. 47 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:240: Gly His Asn His Pro Val Trp Asp Val Ser PheSer Pro Leu Gly His 1 5 10 15 Tyr Phe Ala Thr Ala Ser His Asp Gln ThrAla Arg Leu Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:241: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: TUP1 HOMOLOG rIV, Fig. 47 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:241: Gly His Leu Asn Asp Val Asp Cys Val Ser Phe His Pro AsnGly Cys 1 5 10 15 Tyr Val Phe Thr Gly Ser Ser Asp Lys Thr Cys Arg MetTrp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:242: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: TUP1HOMOLOG rV, Fig. 47 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:242: Gly HisThr Ala Pro Val Ile Ser Ile Ala Val Cys Pro Asp Gly Arg 1 5 10 15 TrpLeu Ser Thr Gly Ser Glu Asp Gly Ile Ile Asn Val Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:243: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: TUP1 HOMOLOG rVI, Fig. 47 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:243: Gly His Gly Lys Asn Ala Ile Tyr Ser Leu SerTyr Ser Lys Glu Gly 1 5 10 15 Asn Val Leu Ile Ser Gly Gly Ala Asp HisThr Val Arg Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:244: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YCU7 rI, Fig. 48 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:244: Gly His Phe Asp Ser Thr Asn Ser Leu Ala Tyr Ser Pro Asp Gly Ser1 5 10 15 Arg Val Val Thr Ala Ser Glu Asp Gly Lys Ile Lys Val Trp Asp 2025 30 (2) INFORMATION FOR SEQ ID NO:245: (i) SEQUENCE CHARACTERISTICS:(A) LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown(ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO(vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCU7 rII, Fig. 48 (xi)SEQUENCE DESCRIPTION: SEQ ID NO:245: Glu His Thr Ser Ser Val Thr Ala ValGln Phe Ala Lys Arg Gly Gln 1 5 10 15 Val Met Phe Ser Ser Ser Leu AspGly Thr Val Arg Ala Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:246:(i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 30 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YCU7 rIII, Fig. 48 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:246: Arg Ile Gln Phe Asn Cys Leu Ala Val Asp Pro Ser Gly Glu Val Val1 5 10 15 Cys Ala Gly Ser Leu Asp Asn Phe Asp Ile His Val Trp Ser 20 2530 (2) INFORMATION FOR SEQ ID NO:247: (i) SEQUENCE CHARACTERISTICS: (A)LENGTH: 31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCU7 rIV, Fig. 48 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:247: Gly His Glu Gly Pro Val Ser Cys Leu Ser PheSer Gln Glu Asn Ser 1 5 10 15 Val Leu Ala Ser Ala Ser Trp Asp Lys ThrIle Arg Ile Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:248: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YCW2 PROTEIN rI, Fig. 49 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:248: Gly His Gly Ser Thr Ile Leu Cys Ser Ala Phe Ala Pro HisThr Ser 1 5 10 15 Ser Arg Met Val Thr Gly Ala Gly Asp Asn Thr Ala ArgIle Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:249: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCW2PROTEIN rII, Fig. 49 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:249: Gly HisTyr Asn Trp Val Leu Cys Val Ser Trp Ser Pro Asp Gly Glu 1 5 10 15 ValIle Ala Thr Gly Ser Met Asp Asn Thr Ile Arg Leu Trp Asp 20 25 30 (2)INFORMATION FOR SEQ ID NO:250: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:38 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: YCW2 PROTEIN rIII, Fig. 49 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:250: Gly His Ser Lys Trp Ile Thr Ser Leu Ser TrpGlu Pro Ile His Leu 1 5 10 15 Val Lys Pro Gly Ser Lys Pro Arg Leu AlaSer Ser Ser Lys Asp Gly 20 25 30 Thr Ile Lys Ile Trp Asp 35 (2)INFORMATION FOR SEQ ID NO:251: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:30 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: YCW2 PROTEIN rIV, Fig. 49 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:251: Gly His Thr Asn Ser Val Ser Cys Val Lys TrpGly Gly Gln Gly Leu 1 5 10 15 Leu Tyr Ser Gly Ser His Asp Arg Thr ValArg Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:252: (i) SEQUENCECHARACTERISTICS: (A) LENGTH: 26 amino acids (B) TYPE: amino acid (D)TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO(iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: YCW2PROTEIN rV, Fig. 49 (xi) SEQUENCE DESCRIPTION: SEQ ID NO:252: Lys IleCys Lys Lys Asn Gly Asn Ser Glu Glu Met Met Val Thr Ala 1 5 10 15 SerAsp Asp Tyr Thr Met Phe Leu Trp Asn 20 25 (2) INFORMATION FOR SEQ IDNO:253: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 25 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YCW2 PROTEIN rVI, Fig. 49 (xi) SEQUENCE DESCRIPTION:SEQ ID NO:253: Asn His Val Ala Phe Ser Pro Asp Gly Arg Tyr Ile Val SerAla Ser 1 5 10 15 Phe Asp Asn Ser Ile Lys Leu Trp Asp 20 25 (2)INFORMATION FOR SEQ ID NO:254: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:31 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: YCW2 PROTEIN rVII, Fig. 49 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:254: Gly His Ile Ala Ser Val Tyr Gln Val Ala TrpSer Ser Asp Cys Arg 1 5 10 15 Leu Leu Val Ser Cys Ser Lys Asp Thr ThrLeu Lys Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:255: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 35 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YCW2 PROTEIN rVIII, Fig. 49 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:255: Ser Val Asp Leu Pro Gly Ile Lys Thr Lys LeuTyr Val Asp Trp Ser 1 5 10 15 Val Asp Gly Lys Arg Val Cys Ser Gly GlyLys Asp Lys Met Val Arg 20 25 30 Leu Trp Thr 35 (2) INFORMATION FOR SEQID NO:256: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 29 amino acids (B)TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: YKL525 rI, Fig. 50 (xi) SEQUENCE DESCRIPTION: SEQ IDNO:256: Leu His Leu Tyr Ala Pro Val Phe Tyr Ser Asp Val Phe Arg Val Phe1 5 10 15 Met Glu His Ala Leu Asp Ile Leu Asp Ala Asn Trp Ser 20 25 (2)INFORMATION FOR SEQ ID NO:257: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH:32 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULETYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: YKL525 rII, Fig. 50 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:257: Val His Pro Asp Phe Val Thr Ser Ala Ile PhePhe Pro Asn Asp Asp 1 5 10 15 Arg Phe Ile Ile Thr Gly Cys Leu Asp HisArg Cys Arg Leu Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:258: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: yrb 1410 yeast rI, Fig. 51 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:258: Gly His Asn His Pro Val Trp Asp Val Ser PheSer Pro Leu Gly His 1 5 10 15 Tyr Phe Ala Thr Ala Ser His Asp Gln ThrAla Arg Leu Trp Ser 20 25 30 (2) INFORMATION FOR SEQ ID NO:259: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: yrb 1410 yeast rII, Fig. 51 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:259: Gly His Leu Asn Asp Val Asp Cys Val Ser PheHis Pro Asn Gly Cys 1 5 10 15 Tyr Val Phe Thr Gly Ser Ser Asp Lys ThrCys Arg Met Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:260: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 31 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: yrb 1410 yeast rIII, Fig. 51 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:260: Gly His Thr Ala Pro Val Ile Ser Ile Ala ValCys Pro Asp Gly Arg 1 5 10 15 Trp Leu Ser Thr Gly Ser Glu Asp Gly IleIle Asn Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:261: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 32 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: yrb 1410 yeast rIV, Fig. 51 (xi) SEQUENCEDESCRIPTION: SEQ ID NO:261: Gly His Gly Lys Asn Ala Ile Tyr Ser Leu SerTyr Ser Lys Glu Gly 1 5 10 15 Asn Val Leu Ile Ser Gly Gly Ala Asp HisThr Val Arg Val Trp Asp 20 25 30 (2) INFORMATION FOR SEQ ID NO:262: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 34 amino acids (B) TYPE: aminoacid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii)HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (C)INDIVIDUAL ISOLATE: WD40 Consensus Sequence (xi) SEQUENCE DESCRIPTION:SEQ ID NO:262: Gly His Ser Ala Ala Leu Ala Ala Leu Ala Leu Ser Pro AspAla Ala 1 5 10 15 Ala Ala Ala Leu Ala Ser Gly Ala Arg Asp Ala Thr LeuArg Leu Trp 20 25 30 Asp Leu (2) INFORMATION FOR SEQ ID NO:263: (i)SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid(C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE:peptide (iii) HYPOTHETICAL: YES (iv) ANTI-SENSE: NO (vi) ORIGINALSOURCE: (C) INDIVIDUAL ISOLATE: WRTAA peptide (xi) SEQUENCE DESCRIPTION:SEQ ID NO:263: Trp Arg Thr Ala Ala 1 5 (2) INFORMATION FOR SEQ IDNO:264: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B)TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: YES (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: WRTAV peptide (xi) SEQUENCEDESCRIPTION: SEQ ID NO:264: Trp Arg Thr Ala Val 1 5 (2) INFORMATION FORSEQ ID NO:265: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids(B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii)MOLECULE TYPE: peptide (iii) HYPOTHETICAL: YES (iv) ANTI-SENSE: NO (vi)ORIGINAL SOURCE: (C) INDIVIDUAL ISOLATE: WRTA peptide (xi) SEQUENCEDESCRIPTION: SEQ ID NO:265: Trp Arg Thr Ala 1

What is claimed is:
 1. A method to identify a compound which willmodulate the localized enzymatic activity of a first target protein thatinteracts with a second protein containing at least one WD-40 regionwhich method comprises determining the interaction of said first andsecond protein containing at least one WD-40 region in the presence andabsence of a candidate compound; comparing the level of interaction ofsaid first and second protein in the presence and absence of saidcandidate compound; and identifying as a successful candidate a compoundwhich modifies the level of interaction of said first and second proteinin its presence as opposed to its absence, wherein the first targetprotein is selected from the group consisting of protein kinase C (PKC)and β adrenergic receptor kinase (βARK) and wherein the WD40 region hasthe amino acid sequence set forth in SEQ ID NO:69-SEQ ID NO:75, thesequence set forth in SEQ ID NO:28-SEQ ID NO:68 or the sequence setforth in SEQ ID NO:128-SEQ ID NO:134.
 2. The method of claim 1 whereinthe first target protein is a protein kinase C (PKC).
 3. The method ofclaim 1 wherein the first target protein is a β adrenergic receptorkinase (βARK).
 4. The method of claim 1 wherein the second protein is areceptor for activated protein kinase C (RACK).
 5. The method of claim 4wherein the second protein has the sequence represented by SEQ ID NO:27.6. A method to identify a compound which modulates the localizedenzymatic activity of a first target protein which interacts with asecond protein containing at least one WD-40 region which methodcomprises determining the interaction between said first target proteinand a peptide of 4-50 amino acids, said peptide having an amino acidsequence derived from the amino acid sequence of the same length in saidWD-40 region of said second protein, in the presence and absence of acandidate compound; comparing the level of interaction of said first andsecond protein in the presence and absence of said candidate compound;and identifying as a successful candidate a compound which modifies thelevel of said interaction in its presence as compared to its absence,wherein the first target protein is selected from the group consistingof protein kinase C (PKC) and β adrenergic receptor kinase (βARK) andwherein the WD-40 region has the amino acid sequence set forth in SEQ IDNO:69-SEQ ID NO:75, the sequence set forth in SEQ ID NO:28-SEQ ID NO:68or the sequence set forth in SEQ ID NO:128-SEQ ID NO:134.
 7. The methodof claim 6 wherein the first target protein is a protein kinase C (PKC).8. The method of claim 6 wherein the first target protein is a βadrenergic receptor kinase (βARK).
 9. The method of claim 6 wherein theWD-40 region has the amino acid sequence set forth in SEQ ID NO:69-SEQID NO:75.
 10. The method of claim 6 wherein the WD-40 region has theamino acid sequence set forth in SEQ ID NO:28-SEQ ID NO:68.
 11. Themethod of claim 6 wherein the WD-40 region has the amino acid sequenceset forth in SEQ ID NO:128-SEQ ID NO:134.
 12. The method of claim 6wherein the peptide has the amino acid sequence set forth in SEQ IDNO:13-SEQ ID NO:18.
 13. The method of claim 6 wherein the peptide hasthe amino acid sequence set forth in SEQ ID NO:4 or SEQ ID NO:7.